PDBsum entry 1huc

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protein Protein-protein interface(s) links
Thiol protease PDB id
Protein chains
47 a.a. *
205 a.a. *
Waters ×283
* Residue conservation analysis
PDB id:
Name: Thiol protease
Title: The refined 2.15 angstroms x-ray crystal structure of human liver cathepsin b: the structural basis for its specificity
Structure: Cathepsin b. Chain: a, c. Engineered: yes. Cathepsin b. Chain: b, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Biol. unit: Hetero-Dimer (from PQS)
2.10Å     R-factor:   0.164    
Authors: D.Musil,W.Bode
Key ref: D.Musil et al. (1991). The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J, 10, 2321-2330. PubMed id: 1868826
21-Apr-93     Release date:   26-Jan-95    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P07858  (CATB_HUMAN) -  Cathepsin B
339 a.a.
47 a.a.
Protein chains
Pfam   ArchSchema ?
P07858  (CATB_HUMAN) -  Cathepsin B
339 a.a.
205 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.  - Cathepsin B.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     cysteine-type peptidase activity     1 term  


EMBO J 10:2321-2330 (1991)
PubMed id: 1868826  
The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.
D.Musil, D.Zucic, D.Turk, R.A.Engh, I.Mayr, R.Huber, T.Popovic, V.Turk, T.Towatari, N.Katunuma.
From the lysosomal cysteine proteinase cathepsin B, isolated from human liver in its two-chain form, monoclinic crystals were obtained which contain two molecules per asymmetric unit. The molecular structure was solved by a combination of Patterson search and heavy atom replacement methods (simultaneously with rat cathepsin B) and refined to a crystallographic R value of 0.164 using X-ray data to 2.15 A resolution. The overall folding pattern of cathepsin B and the arrangement of the active site residues are similar to the related cysteine proteinases papain, actinidin and calotropin DI. 166 alpha-carbon atoms out of 248 defined cathepsin B residues are topologically equivalent (with an r.m.s. deviation of 1.04 A) with alpha-carbon atoms of papain. However, several large insertion loops are accommodated on the molecular surface and modify its properties. The disulphide connectivities recently determined for bovine cathepsin B by chemical means were shown to be correct. Some of the primed subsites are occluded by a novel insertion loop, which seems to favour binding of peptide substrates with two residues carboxy-terminal to the scissile peptide bond; two histidine residues (His110 and His111) in this "occluding loop' provide positively charged anchors for the C-terminal carboxylate group of such polypeptide substrates. These structural features explain the well-known dipeptidyl carboxypeptidase activity of cathepsin B. The other subsites adjacent to the reactive site Cys29 are relatively similar to papain; Glu245 in the S2 subsite favours basic P2-side chains. The above mentioned histidine residues, but also the buried Glu171 might represent the group with a pKa of approximately 5.5 near the active site, which governs endo- and exopeptidase activity. The "occluding loop' does not allow cystatin-like protein inhibitors to bind to cathepsin B as they do to papain, consistent with the reduced affinity of these protein inhibitors for cathepsin B compared with the related plant enzymes.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21360607 H.C.Castro, P.A.Abreu, R.B.Geraldo, R.C.Martins, R.Dos Santos, N.I.Loureiro, L.M.Cabral, and C.R.Rodrigues (2011).
Looking at the proteases from a simple perspective.
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21321730 K.P.Bhabak, B.J.Bhuyan, and G.Mugesh (2011).
Bioinorganic and medicinal chemistry: aspects of gold(i)-protein complexes.
  Dalton Trans, 40, 2099-2111.  
21321479 N.Katunuma (2011).
Structure-based development of specific inhibitors for individual cathepsins and their medical applications.
  Proc Jpn Acad Ser B Phys Biol Sci, 87, 29-39.  
20361051 A.Rennenberg, C.Lehmann, A.Heitmann, T.Witt, G.Hansen, K.Nagarajan, C.Deschermeier, V.Turk, R.Hilgenfeld, and V.T.Heussler (2010).
Exoerythrocytic Plasmodium parasites secrete a cysteine protease inhibitor involved in sporozoite invasion and capable of blocking cell death of host hepatocytes.
  PLoS Pathog, 6, e1000825.  
20980477 H.Kido, and K.Ishidoh (2010).
Nobuhiko Katunuma: an outstanding scientist in the field of proteolysis and warm-hearted 'Kendo Fighter' biochemist.
  J Biochem, 148, 527-531.  
20048156 J.E.Ahn, L.A.Guarino, and K.Zhu-Salzman (2010).
Coordination of hepatocyte nuclear factor 4 and seven-up controls insect counter-defense cathepsin B expression.
  J Biol Chem, 285, 6573-6584.  
20652927 L.Mendieta, A.Picó, T.Tarragó, M.Teixidó, M.Castillo, L.Rafecas, A.Moyano, and E.Giralt (2010).
Novel peptidyl aryl vinyl sulfones as highly potent and selective inhibitors of cathepsins L and B.
  ChemMedChem, 5, 1556-1567.  
21210971 M.G.Costa, P.R.Batista, C.S.Shida, C.H.Robert, P.M.Bisch, and P.G.Pascutti (2010).
How does heparin prevent the pH inactivation of cathepsin B? Allosteric mechanism elucidated by docking and molecular dynamics.
  BMC Genomics, 11, S5.  
20860624 M.Renko, U.Požgan, D.Majera, and D.Turk (2010).
Stefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleft.
  FEBS J, 277, 4338-4345.
PDB code: 3k9m
20060836 N.Chim, R.Riley, J.The, S.Im, B.Segelke, T.Lekin, M.Yu, L.W.Hung, T.Terwilliger, J.P.Whitelegge, and C.W.Goulding (2010).
An extracellular disulfide bond forming protein (DsbF) from Mycobacterium tuberculosis: structural, biochemical, and gene expression analysis.
  J Mol Biol, 396, 1211-1226.
PDB code: 3ios
19656187 B.Mirković, A.Premzl, V.Hodnik, B.Doljak, Z.Jevnikar, G.Anderluh, and J.Kos (2009).
Regulation of cathepsin B activity by 2A2 monoclonal antibody.
  FEBS J, 276, 4739-4751.  
19361282 C.Serbielle, S.Moreau, F.Veillard, E.Voldoire, A.Bézier, M.A.Mannucci, A.N.Volkoff, J.M.Drezen, G.Lalmanach, and E.Huguet (2009).
Identification of parasite-responsive cysteine proteases in Manduca sexta.
  Biol Chem, 390, 493-502.  
18708063 K.Dolecková, M.Kasný, L.Mikes, J.Cartwright, P.Jedelský, E.L.Schneider, J.Dvorák, A.P.Mountford, C.S.Craik, and P.Horák (2009).
The functional expression and characterisation of a cysteine peptidase from the invasive stage of the neuropathogenic schistosome Trichobilharzia regenti.
  Int J Parasitol, 39, 201-211.  
19401154 S.A.Beckham, D.Piedrafita, C.I.Phillips, N.Samarawickrema, R.H.Law, P.M.Smooker, N.S.Quinsey, J.A.Irving, D.Greenwood, S.H.Verhelst, M.Bogyo, B.Turk, T.H.Coetzer, L.C.Wijeyewickrema, T.W.Spithill, and R.N.Pike (2009).
A major cathepsin B protease from the liver fluke Fasciola hepatica has atypical active site features and a potential role in the digestive tract of newly excysted juvenile parasites.
  Int J Biochem Cell Biol, 41, 1601-1612.  
18959767 A.Tsuji, Y.Kikuchi, K.Ogawa, H.Saika, K.Yuasa, and M.Nagahama (2008).
Purification and characterization of cathepsin B-like cysteine protease from cotyledons of daikon radish, Raphanus sativus.
  FEBS J, 275, 5429-5443.  
18281598 C.Mendoza-Palomares, N.Biteau, C.Giroud, V.Coustou, T.Coetzer, E.Authié, A.Boulangé, and T.Baltz (2008).
Molecular and biochemical characterization of a cathepsin B-like protease family unique to Trypanosoma congolense.
  Eukaryot Cell, 7, 684-697.  
18515357 I.Redzynia, A.Ljunggren, M.Abrahamson, J.S.Mort, J.C.Krupa, M.Jaskolski, and G.Bujacz (2008).
Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B.
  J Biol Chem, 283, 22815-22825.
PDB codes: 3cbj 3cbk
18251797 J.B.Dacks, T.Kuru, N.A.Liapounova, and L.Gedamu (2008).
Phylogenetic and primary sequence characterization of cathepsin B cysteine proteases from the oxymonad flagellate monocercomonoides.
  J Eukaryot Microbiol, 55, 9.  
18483546 N.Tsuji, T.Miyoshi, B.Battsetseg, T.Matsuo, X.Xuan, and K.Fujisaki (2008).
A cysteine protease is critical for Babesia spp. transmission in Haemaphysalis ticks.
  PLoS Pathog, 4, e1000062.  
18796695 P.Schenker, P.Alfarano, P.Kolb, A.Caflisch, and A.Baici (2008).
A double-headed cathepsin B inhibitor devoid of warhead.
  Protein Sci, 17, 2145-2155.  
18253767 S.S.Gunatilleke, Oliveira, J.A.McCammon, and A.M.Barrios (2008).
Inhibition of cathepsin B by Au(I) complexes: a kinetic and computational study.
  J Biol Inorg Chem, 13, 555-561.  
18397276 Y.D.Koo, J.E.Ahn, R.A.Salzman, J.Moon, Y.H.Chi, D.J.Yun, S.Y.Lee, H.Koiwa, and K.Zhu-Salzman (2008).
Functional expression of an insect cathepsin B-like counter-defence protein.
  Insect Mol Biol, 17, 235-245.  
18951789 Y.Takeuchi, T.Fujiwara, Y.Shimone, H.Miyataka, T.Satoh, K.L.Kirk, and H.Hori (2008).
Possible involvement of radical intermediates in the inhibition of cysteine proteases by allenyl esters and amides.
  Bioorg Med Chem Lett, 18, 6202-6205.  
17403677 C.M.Stack, S.Donnelly, J.Lowther, W.Xu, P.R.Collins, L.S.Brinen, and J.P.Dalton (2007).
The major secreted cathepsin L1 protease of the liver fluke, Fasciola hepatica: a Leu-12 to Pro-12 replacement in the nonconserved C-terminal region of the prosegment prevents complete enzyme autoactivation and allows definition of the molecular events in prosegment removal.
  J Biol Chem, 282, 16532-16543.  
17726009 D.Caglic, J.R.Pungercar, G.Pejler, V.Turk, and B.Turk (2007).
Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions.
  J Biol Chem, 282, 33076-33085.  
17459103 J.E.Ahn, L.A.Guarino, and K.Zhu-Salzman (2007).
Seven-up facilitates insect counter-defense by suppressing cathepsin B expression.
  FEBS J, 274, 2800-2814.  
17433072 J.E.Ahn, M.R.Lovingshimer, R.A.Salzman, J.K.Presnail, A.L.Lu, H.Koiwa, and K.Zhu-Salzman (2007).
Cowpea bruchid Callosobruchus maculatus counteracts dietary protease inhibitors by modulating propeptides of major digestive enzymes.
  Insect Mol Biol, 16, 295-304.  
17651235 S.Prabhakar, M.S.Chen, E.N.Elpidina, K.S.Vinokurov, C.M.Smith, J.Marshall, and B.Oppert (2007).
Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor L.
  Insect Mol Biol, 16, 455-468.  
17176758 A.Pavlova, K.Krovácek, I.Ciznár, and C.Gonzalez-Rey (2006).
Inhibition of mammalian cathepsins by Plesiomonas shigelloides.
  Folia Microbiol (Praha), 51, 393-400.  
16772304 M.Kotsyfakis, A.Sá-Nunes, I.M.Francischetti, T.N.Mather, J.F.Andersen, and J.M.Ribeiro (2006).
Antiinflammatory and immunosuppressive activity of sialostatin L, a salivary cystatin from the tick Ixodes scapularis.
  J Biol Chem, 281, 26298-26307.  
16990854 M.M.Mohamed, and B.F.Sloane (2006).
Cysteine cathepsins: multifunctional enzymes in cancer.
  Nat Rev Cancer, 6, 764-775.  
16485313 P.Ruzza, L.Quintieri, A.Osler, A.Calderan, B.Biondi, M.Floreani, A.Guiotto, and G.Borin (2006).
Fluorescent, internally quenched, peptides for exploring the pH-dependent substrate specificity of cathepsin B.
  J Pept Sci, 12, 455-461.  
16895475 S.A.Beckham, R.H.Law, P.M.Smooker, N.S.Quinsey, C.R.Caffrey, J.H.McKerrow, R.N.Pike, and T.W.Spithill (2006).
Production and processing of a recombinant Fasciola hepatica cathepsin B-like enzyme (FhcatB1) reveals potential processing mechanisms in the parasite.
  Biol Chem, 387, 1053-1061.  
16982417 S.Mueller-Steiner, Y.Zhou, H.Arai, E.D.Roberson, B.Sun, J.Chen, X.Wang, G.Yu, L.Esposito, L.Mucke, and L.Gan (2006).
Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease.
  Neuron, 51, 703-714.  
16777845 T.Hogg, K.Nagarajan, S.Herzberg, L.Chen, X.Shen, H.Jiang, M.Wecke, C.Blohmke, R.Hilgenfeld, and C.L.Schmidt (2006).
Structural and functional characterization of Falcipain-2, a hemoglobinase from the malarial parasite Plasmodium falciparum.
  J Biol Chem, 281, 25425-25437.
PDB code: 2ghu
16408036 G.Blum, S.R.Mullins, K.Keren, M.Fonovic, C.Jedeszko, M.J.Rice, B.F.Sloane, and M.Bogyo (2005).
Dynamic imaging of protease activity with fluorescently quenched activity-based probes.
  Nat Chem Biol, 1, 203-209.  
16307485 L.Puzer, S.S.Cotrin, M.H.Cezari, I.Y.Hirata, M.A.Juliano, I.Stefe, D.Turk, B.Turk, L.Juliano, and A.K.Carmona (2005).
Recombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L.
  Biol Chem, 386, 1191-1195.  
15728581 M.Alvarez-Fernandez, Y.H.Liang, M.Abrahamson, and X.D.Su (2005).
Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile.
  J Biol Chem, 280, 18221-18228.
PDB codes: 1rn7 1roa
15795757 S.Fuchs, H.Otto, S.Jehle, P.Henklein, and A.D.Schluter (2005).
Fluorescent dendrimers with a peptide cathepsin B cleavage site for drug delivery applications.
  Chem Commun (Camb), (), 1830-1832.  
16172011 S.U.Lim, J.S.Seo, M.S.Kim, S.J.Ahn, H.D.Jeong, K.H.Kim, N.G.Park, J.K.Kim, J.K.Chung, and H.H.Lee (2005).
Molecular cloning and characterization of Cathepsin B from a scuticociliate, Uronema marinum.
  Comp Biochem Physiol B Biochem Mol Biol, 142, 283-292.  
15195995 A.Rossi, Q.Deveraux, B.Turk, and A.Sali (2004).
Comprehensive search for cysteine cathepsins in the human genome.
  Biol Chem, 385, 363-372.  
14755576 D.Peters, and J.Peters (2004).
The ribbon of hydrogen bonds in globular proteins. IV. The example of the papain family.
  Biopolymers, 73, 178-191.  
15157229 J.Moon, R.A.Salzman, J.E.Ahn, H.Koiwa, and K.Zhu-Salzman (2004).
Transcriptional regulation in cowpea bruchid guts during adaptation to a plant defence protease inhibitor.
  Insect Mol Biol, 13, 283-291.  
15574492 K.Wenig, L.Chatwell, U.von Pawel-Rammingen, L.Björck, R.Huber, and P.Sondermann (2004).
Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.
  Proc Natl Acad Sci U S A, 101, 17371-17376.
PDB code: 1y08
14694194 M.Zhu, F.Shao, R.W.Innes, J.E.Dixon, and Z.Xu (2004).
The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site.
  Proc Natl Acad Sci U S A, 101, 302-307.
PDB code: 1ukf
14754899 P.R.Collins, C.M.Stack, S.M.O'Neill, S.Doyle, T.Ryan, G.P.Brennan, A.Mousley, M.Stewart, A.G.Maule, J.P.Dalton, and S.Donnelly (2004).
Cathepsin L1, the major protease involved in liver fluke (Fasciola hepatica) virulence: propetide cleavage sites and autoactivation of the zymogen secreted from gastrodermal cells.
  J Biol Chem, 279, 17038-17046.  
12887049 B.Turk, H.Fritz, and V.Turk (2003).
Vito Turk--30 years of research on cysteine proteases and their inhibitors.
  Biol Chem, 384, 833-836.  
12887050 D.K.Nägler, and R.Ménard (2003).
Family C1 cysteine proteases: biological diversity or redundancy?
  Biol Chem, 384, 837-843.  
12554931 D.Turk, and G.Guncar (2003).
Lysosomal cysteine proteases (cathepsins): promising drug targets.
  Acta Crystallogr D Biol Crystallogr, 59, 203-213.  
14690410 M.E.McGrath, P.A.Sprengeler, C.M.Hill, V.Martichonok, H.Cheung, J.R.Somoza, J.T.Palmer, and J.W.Janc (2003).
Peptide ketobenzoxazole inhibitors bound to cathepsin K.
  Biochemistry, 42, 15018-15028.  
12833545 M.Sulpizi, A.Laio, J.VandeVondele, A.Cattaneo, U.Rothlisberger, and P.Carloni (2003).
Reaction mechanism of caspases: insights from QM/MM Car-Parrinello simulations.
  Proteins, 52, 212-224.  
12668429 M.Sulpizi, U.Rothlisberger, and P.Carloni (2003).
Molecular dynamics studies of caspase-3.
  Biophys J, 84, 2207-2215.  
12887055 N.Katunuma, Y.Matsunaga, K.Himeno, and Y.Hayashi (2003).
Insights into the roles of cathepsins in antigen processing and presentation revealed by specific inhibitors.
  Biol Chem, 384, 883-890.  
14621998 O.Vasiljeva, M.Dolinar, V.Turk, and B.Turk (2003).
Recombinant human cathepsin H lacking the mini chain is an endopeptidase.
  Biochemistry, 42, 13522-13528.  
12784208 S.Biswas, C.Chakrabarti, S.Kundu, M.V.Jagannadham, and J.K.Dattagupta (2003).
Proposed amino acid sequence and the 1.63 A X-ray crystal structure of a plant cysteine protease, ervatamin B: some insights into the structural basis of its stability and substrate specificity.
  Proteins, 51, 489-497.
PDB code: 1iwd
12423365 A.Pavlova, and I.Björk (2002).
The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73.
  Eur J Biochem, 269, 5649-5658.  
11939796 J.A.Irving, R.N.Pike, W.Dai, D.Brömme, D.M.Worrall, G.A.Silverman, T.H.Coetzer, C.Dennison, S.P.Bottomley, and J.C.Whisstock (2002).
Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: engineering alpha(1)-antitrypsin to inhibit cathepsin proteases.
  Biochemistry, 41, 4998-5004.  
11910036 M.Horn, M.Baudys, Z.Voburka, I.Kluh, J.Vondrásek, and M.Mares (2002).
Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I).
  Protein Sci, 11, 933-943.  
11258881 C.Therrien, P.Lachance, T.Sulea, E.O.Purisima, H.Qi, E.Ziomek, A.Alvarez-Hernandez, W.R.Roush, and R.Ménard (2001).
Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities.
  Biochemistry, 40, 2702-2711.  
11726493 D.Turk, V.Janjić, I.Stern, M.Podobnik, D.Lamba, S.W.Dahl, C.Lauritzen, J.Pedersen, V.Turk, and B.Turk (2001).
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases.
  EMBO J, 20, 6570-6582.
PDB code: 1k3b
11514663 E.Pol, and I.Björk (2001).
Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases.
  Protein Sci, 10, 1729-1738.  
11532926 V.Turk, B.Turk, and D.Turk (2001).
Lysosomal cysteine proteases: facts and opportunities.
  EMBO J, 20, 4629-4633.  
10745011 G.Guncar, I.Klemencic, B.Turk, V.Turk, A.Karaoglanovic-Carmona, L.Juliano, and D.Turk (2000).
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.
  Structure, 8, 305-313.
PDB code: 1ef7
10951198 I.Klemencic, A.K.Carmona, M.H.Cezari, M.A.Juliano, L.Juliano, G.Guncar, D.Turk, I.Krizaj, V.Turk, and B.Turk (2000).
Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase.
  Eur J Biochem, 267, 5404-5412.  
11169395 M.Kasai, H.Kropshofer, A.B.Vogt, E.Kominami, and T.Mizuochi (2000).
CLIP-derived self peptides bound to MHC class II molecules of medullary thymic epithelial cells differ from those of cortical thymic epithelial cells in their diversity, length, and C-terminal processing.
  Eur J Immunol, 30, 3542-3551.  
11667982 P.J.Wolters, and H.A.Chapman (2000).
Importance of lysosomal cysteine proteases in lung disease.
  Respir Res, 1, 170-177.  
10716634 R.I.Brinkworth, J.F.Tort, P.J.Brindley, and J.P.Dalton (2000).
Phylogenetic relationships and theoretical model of human cathepsin W (lymphopain), a cysteine proteinase from cytotoxic T lymphocytes.
  Int J Biochem Cell Biol, 32, 373-384.  
  11152132 S.Estrada, S.T.Olson, E.Raub-Segall, and I.Björk (2000).
The N-terminal region of cystatin A (stefin A) binds to papain subsequent to the two hairpin loops of the inhibitor. Demonstration of two-step binding by rapid-kinetic studies of cystatin A labeled at the N-terminus with a fluorescent reporter group.
  Protein Sci, 9, 2218-2224.  
10840150 T.Yamashima (2000).
Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates.
  Prog Neurobiol, 62, 273-295.  
10708750 V.Stoka, B.Turk, J.H.McKerrow, I.Björk, J.J.Cazzulo, and V.Turk (2000).
The high stability of cruzipain against pH-induced inactivation is not dependent on its C-terminal domain.
  FEBS Lett, 469, 29-32.  
10491143 B.Cigic, and R.H.Pain (1999).
Location of the binding site for chloride ion activation of cathepsin C.
  Eur J Biochem, 264, 944-951.  
10447678 B.E.Linebaugh, M.Sameni, N.A.Day, B.F.Sloane, and D.Keppler (1999).
Exocytosis of active cathepsin B enzyme activity at pH 7.0, inhibition and molecular mass.
  Eur J Biochem, 264, 100-109.  
10350606 C.Czaplewski, Z.Grzonka, M.Jaskólski, F.Kasprzykowski, M.Kozak, E.Politowska, and J.Ciarkowski (1999).
Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?
  Biochim Biophys Acta, 1431, 290-305.  
10200176 D.K.Nägler, W.Tam, A.C.Storer, J.C.Krupa, J.S.Mort, and R.Ménard (1999).
Interdependency of sequence and positional specificities for cysteine proteases of the papain family.
  Biochemistry, 38, 4868-4874.  
10022822 G.Guncar, G.Pungercic, I.Klemencic, V.Turk, and D.Turk (1999).
Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S.
  EMBO J, 18, 793-803.
PDB code: 1icf
10383408 J.A.Schmid, L.Mach, E.Paschke, and J.Glössl (1999).
Accumulation of sialic acid in endocytic compartments interferes with the formation of mature lysosomes. Impaired proteolytic processing of cathepsin B in fibroblasts of patients with lysosomal sialic acid storage disease.
  J Biol Chem, 274, 19063-19071.  
10631941 J.A.Villadangos, R.A.Bryant, J.Deussing, C.Driessen, A.M.Lennon-Duménil, R.J.Riese, W.Roth, P.Saftig, G.P.Shi, H.A.Chapman, C.Peters, and H.L.Ploegh (1999).
Proteases involved in MHC class II antigen presentation.
  Immunol Rev, 172, 109-120.  
10373004 J.C.Whisstock, J.A.Irving, S.P.Bottomley, R.N.Pike, and A.M.Lesk (1999).
Serpins in the Caenorhabditis elegans genome.
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10380357 K.Matsumoto, K.Mizoue, K.Kitamura, W.C.Tse, C.P.Huber, and T.Ishida (1999).
Structural basis of inhibition of cysteine proteases by E-64 and its derivatives.
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10215884 K.Ylinenjärvi, M.Widersten, and I.Björk (1999).
Hydrophobic sequences can substitute for the wild-type N-terminal sequence of cystatin A (stefin A) in tight binding to cysteine proteinases selection of high-affinity N-terminal region variants by phage display.
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10425337 M.Dvorák, P.Kopecková, and J.Kopecek (1999).
High-molecular weight HPMA copolymer-adriamycin conjugates.
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10410800 M.E.McGrath (1999).
The lysosomal cysteine proteases.
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10470376 N.Katunuma, A.Matsui, T.Kakegawa, E.Murata, T.Asao, and Y.Ohba (1999).
Study of the functional share of lysosomal cathepsins by the development of specific inhibitors.
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10213604 O.Quraishi, D.K.Nägler, T.Fox, J.Sivaraman, M.Cygler, J.S.Mort, and A.C.Storer (1999).
The occluding loop in cathepsin B defines the pH dependence of inhibition by its propeptide.
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The contribution of N-terminal region residues of cystatin A (stefin A) to the affinity and kinetics of inhibition of papain, cathepsin B, and cathepsin L.
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10196232 T.Okamoto, T.Minamikawa, G.Edward, V.Vakharia, E.Herman, and T.Okomoto (1999).
Posttranslational removal of the carboxyl-terminal KDEL of the cysteine protease SH-EP occurs prior to maturation of the enzyme.
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10380356 T.Schirmeister (1999).
Inhibition of cysteine proteases by peptides containing aziridine-2,3-dicarboxylic acid building blocks.
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10224092 W.L.Cho, S.M.Tsao, A.R.Hays, R.Walter, J.S.Chen, E.S.Snigirevskaya, and A.S.Raikhel (1999).
Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin is produced as a latent extraovarian precursor.
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9776083 A.A.Sinha, B.J.Quast, M.J.Wilson, P.K.Reddy, D.F.Gleason, and B.F.Sloane (1998).
Codistribution of procathepsin B and mature cathepsin B forms in human prostate tumors detected by confocal and immunofluorescence microscopy.
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9822672 B.Wang, G.P.Shi, P.M.Yao, Z.Li, H.A.Chapman, and D.Brömme (1998).
Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization.
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9493267 G.Guncar, M.Podobnik, J.Pungercar, B.Strukelj, V.Turk, and D.Turk (1998).
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.
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PDB code: 8pch
9523118 H.A.Chapman (1998).
Endosomal proteolysis and MHC class II function.
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9642240 I.Santamaría, G.Velasco, A.M.Pendás, A.Fueyo, and C.López-Otín (1998).
Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location.
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Crystal structure of human cathepsin S.
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9620612 M.Meldal, I.B.Svendsen, L.Juliano, M.A.Juliano, E.D.Nery, and J.Scharfstein (1998).
Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. D-amino acid inhibitors for cruzipain, cathepsin B and cathepsin L.
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Novel physiological functions of cathepsins B and L on antigen processing and osteoclastic bone resorption.
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9585570 S.Estrada, M.Nycander, N.J.Hill, C.J.Craven, J.P.Waltho, and I.Björk (1998).
The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L.
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9582368 S.Mehtani, Q.Gong, J.Panella, S.Subbiah, D.M.Peffley, and A.Frankfater (1998).
In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. Subcellular distribution of the truncated enzyme in COS cells.
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9788682 W.R.Thomas, and W.Smith (1998).
House-dust-mite allergens.
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Experimental measurement of the effective dielectric in the hydrophobic core of a protein.
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Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain.
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9033588 B.Zhao, C.A.Janson, B.Y.Amegadzie, K.D'Alessio, C.Griffin, C.R.Hanning, C.Jones, J.Kurdyla, M.McQueney, X.Qiu, W.W.Smith, and S.S.Abdel-Meguid (1997).
Crystal structure of human osteoclast cathepsin K complex with E-64.
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PDB code: 1atk
8995421 C.Illy, O.Quraishi, J.Wang, E.Purisima, T.Vernet, and J.S.Mort (1997).
Role of the occluding loop in cathepsin B activity.
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Inhibition of papain with 2-benzyl-3,4-epoxybutanoic acid esters. Mechanistic and stereochemical probe for cysteine protease catalysis.
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A possible role for cathepsins D, E, and B in the processing of beta-amyloid precursor protein in Alzheimer's disease.
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Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzyme.
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Emerging roles for cysteine proteases in human biology.
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Cathepsin B.
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Crystal structure of human cathepsin K complexed with a potent inhibitor.
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PDB code: 1mem
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E-64 analogues as inhibitors of cathepsin B. On the role of the absolute configuration of the epoxysuccinyl group.
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Structural determinants of specificity in the cysteine protease cruzain.
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PDB codes: 1aim 2aim
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The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.
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A primitive enzyme for a primitive cell: the protease required for excystation of Giardia.
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Studies on activation and inhibition of cathepsin B from buffalo liver.
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Contribution to activity of histidine-aromatic, amide-aromatic, and aromatic-aromatic interactions in the extended catalytic site of cysteine proteinases.
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8973203 D.Maes, J.Bouckaert, F.Poortmans, L.Wyns, and Y.Looze (1996).
Structure of chymopapain at 1.7 A resolution.
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PDB code: 1yal
8654398 E.A.Auerswald, D.K.Nägler, S.Gross, I.Assfalg-Machleidt, M.T.Stubbs, C.Eckerskorn, W.Machleidt, and H.Fritz (1996).
Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B.
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The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases.
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Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion.
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PDB code: 1mir
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Rapid kinetic studies and structural determination of a cysteine proteinase mutant imply that residue 158 in caricain has a major effect upon the ability of the active site histidine to protonate a dipyridyl probe.
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Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.
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PDB code: 1cjl
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Tumor protease-activated, pore-forming toxins from a combinatorial library.
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Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs.
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PDB code: 1bhg
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Cys102 and His398 are required for bleomycin-inactivating activity but not for hexamer formation of yeast bleomycin hydrolase.
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Cathepsin B in angiogenesis of human prostate: an immunohistochemical and immunoelectron microscopic analysis.
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Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases.
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Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins.
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Quantification of intracellular cathepsin activities in human lung tumor cell lines by flow cytometry.
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Three-dimensional structure of human lysosomal aspartylglucosaminidase.
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PDB codes: 1apy 1apz
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Conserved cystatin segments as models for designing specific substrates and inhibitors of cysteine proteinases.
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Identification of two novel Dictyostelium discoideum cysteine proteinases that carry N-acetylglucosamine-1-P-modification.
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Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism.
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PDB code: 1ivy
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The preparation of catalytically active human cathepsin B from its precursor expressed in Escherichia coli in the form of inclusion bodies.
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The structure of the bovine cathepsin B gene. Genetic variability in the 3' untranslated region.
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7890671 Z.Jia, S.Hasnain, T.Hirama, X.Lee, J.S.Mort, R.To, and C.P.Huber (1995).
Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design.
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PDB codes: 1cpj 1cte 1the
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Structure/function implications for the aminopeptidase specificity of aleurain.
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Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer.
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Elongation on the amino-terminal part of stefin B decreases inhibition of cathepsin H.
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Two crystal structures for cathepsin D: the lysosomal targeting signal and active site.
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Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes.
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Recombinant chicken egg white cystatin variants of the QLVSG region.
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A gibberellin-regulated gene from wheat with sequence homology to cathepsin B of mammalian cells.
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Studies on the aminopeptidase activity of rat cathepsin H.
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