PDBsum entry 1cjl

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protein links
Hydrolase PDB id
Protein chain
307 a.a. *
Waters ×213
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of a cysteine protease proform
Structure: Procathepsin l. Chain: a. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: human cdna. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Other_details: first residue (thr) changed to ser
2.20Å     R-factor:   0.182     R-free:   0.241
Authors: R.Coulombe,P.Grochulski,J.Sivaraman,M.Cygler
Key ref: R.Coulombe et al. (1996). Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J, 15, 5492-5503. PubMed id: 8896443
24-Jul-96     Release date:   12-Aug-97    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P07711  (CATL1_HUMAN) -  Cathepsin L1
333 a.a.
307 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Cathepsin L.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   7 terms 
  Biological process     macrophage apoptotic process   12 terms 
  Biochemical function     protein binding     10 terms  


EMBO J 15:5492-5503 (1996)
PubMed id: 8896443  
Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.
R.Coulombe, P.Grochulski, J.Sivaraman, R.Ménard, J.S.Mort, M.Cygler.
Cathepsin L is a member of the papain superfamily of cysteine proteases and, like many other proteases, it is synthesized as an inactive proenzyme. Its prosegment shows little homology to that of procathepsin B, whose structure, the first for a cysteine protease proenzyme, has been determined recently. We report here the 3-D structure of a mutant of human procathepsin L determined at 2.2 A resolution, describe the mode of binding employed by the prosegment and discuss the molecular basis for other possible roles of the prosegment. The N-terminal part of the prosegment is globular and contains three alpha-helices with a small hydrophobic core built around aromatic side chains. This domain packs against a loop on the enzyme's surface, with the aromatic side chain from the prosegment being located in the center of this loop and providing a large contact area. The C-terminal portion of the prosegment assumes an extended conformation and follows along the substrate binding cleft toward the N-terminus of the mature enzyme. The direction of the prosegment in the substrate binding cleft is opposite to that of substrates. The previously described role of the prosegment in the interactions with membranes is supported by the structure of its N-terminal domain. The fold of the prosegment and the mechanism by which it inhibits the enzymatic activity of procathepsin L is similar to that observed in procathepsin B despite differences in length and sequence, suggesting that this mode of inhibition is common to all enzymes from the papain superfamily.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21245911 R.M.Morphew, H.A.Wright, E.J.Lacourse, J.Porter, J.Barrett, D.J.Woods, and P.M.Brophy (2011).
Towards delineating functions within the fasciola secreted cathepsin l protease family by integrating in vivo based sub-proteomics and phylogenetics.
  PLoS Negl Trop Dis, 5, e937.  
20123797 E.B.Chuong, W.Tong, and H.E.Hoekstra (2010).
Maternal-fetal conflict: rapidly evolving proteins in the rodent placenta.
  Mol Biol Evol, 27, 1221-1225.  
20921628 J.Reiser, B.Adair, and T.Reinheckel (2010).
Specialized roles for cysteine cathepsins in health and disease.
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20964874 M.Bleischwitz, M.Albert, H.L.Fuchsbauer, and R.Kaldenhoff (2010).
Significance of Cuscutain, a cysteine protease from Cuscuta reflexa, in host-parasite interactions.
  BMC Plant Biol, 10, 227.  
19910310 R.M.Deshapriya, S.Yuhashi, M.Usui, T.Kageyama, and Y.Yamamoto (2010).
Identification of essential residues of CTLA-2alpha for inhibitory potency.
  J Biochem, 147, 393-404.  
19091155 B.K.Na, J.M.Kang, H.I.Cheun, S.H.Cho, S.U.Moon, T.S.Kim, and W.M.Sohn (2009).
Cryptopain-1, a cysteine protease of Cryptosporidium parvum, does not require the pro-domain for folding.
  Parasitology, 136, 149-157.  
19596863 E.T.Larson, F.Parussini, M.H.Huynh, J.D.Giebel, A.M.Kelley, L.Zhang, M.Bogyo, E.A.Merritt, and V.B.Carruthers (2009).
Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl.
  J Biol Chem, 284, 26839-26850.
PDB code: 3f75
19172172 J.Lowther, M.W.Robinson, S.M.Donnelly, W.Xu, C.M.Stack, J.M.Matthews, and J.P.Dalton (2009).
The Importance of pH in Regulating the Function of the Fasciola hepatica Cathepsin L1 Cysteine Protease.
  PLoS Negl Trop Dis, 3, e369.  
19143833 J.R.Pungercar, D.Caglic, M.Sajid, M.Dolinar, O.Vasiljeva, U.Pozgan, D.Turk, M.Bogyo, V.Turk, and B.Turk (2009).
Autocatalytic processing of procathepsin B is triggered by proenzyme activity.
  FEBS J, 276, 660-668.  
19479029 K.C.Pandey, D.T.Barkan, A.Sali, and P.J.Rosenthal (2009).
Regulatory elements within the prodomain of falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparum.
  PLoS One, 4, e5694.  
19040358 K.Schilling, A.Körner, S.Sehmisch, A.Kreusch, R.Kleint, Y.Benedix, A.Schlabrakowski, and B.Wiederanders (2009).
Selectivity of propeptide-enzyme interaction in cathepsin L-like cysteine proteases.
  Biol Chem, 390, 167-174.  
19443417 M.W.Robinson, R.Menon, S.M.Donnelly, J.P.Dalton, and S.Ranganathan (2009).
An integrated transcriptomics and proteomics analysis of the secretome of the helminth pathogen Fasciola hepatica: proteins associated with invasion and infection of the mammalian host.
  Mol Cell Proteomics, 8, 1891-1907.  
19308250 P.Pinlaor, N.Kaewpitoon, T.Laha, B.Sripa, S.Kaewkes, M.E.Morales, V.H.Mann, S.K.Parriott, S.Suttiprapa, M.W.Robinson, J.To, J.P.Dalton, A.Loukas, and P.J.Brindley (2009).
Cathepsin F Cysteine Protease of the Human Liver Fluke, Opisthorchis viverrini.
  PLoS Negl Trop Dis, 3, e398.  
18160404 C.M.Stack, C.R.Caffrey, S.M.Donnelly, A.Seshaadri, J.Lowther, J.F.Tort, P.R.Collins, M.W.Robinson, W.Xu, J.H.McKerrow, C.S.Craik, S.R.Geiger, R.Marion, L.S.Brinen, and J.P.Dalton (2008).
Structural and functional relationships in the virulence-associated cathepsin L proteases of the parasitic liver fluke, Fasciola hepatica.
  J Biol Chem, 283, 9896-9908.
PDB code: 2o6x
18445589 K.N.DuBois, M.Abodeely, J.Sakanari, C.S.Craik, M.Lee, J.H.McKerrow, and M.Sajid (2008).
Identification of the major cysteine protease of Giardia and its role in encystation.
  J Biol Chem, 283, 18024-18031.  
18379686 M.Fairhead, K.A.Johnson, T.Kowatz, S.A.McMahon, L.G.Carter, M.Oke, H.Liu, J.H.Naismith, and C.F.van der Walle (2008).
Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras.
  Chem Commun (Camb), 15, 1765-1767.
PDB code: 2vhs
18503638 M.J.Blackman (2008).
Malarial proteases and host cell egress: an 'emerging' cascade.
  Cell Microbiol, 10, 1925-1934.  
18551692 N.Schaschke, I.Assfalg-Machleidt, and W.Machleidt (2008).
Inhibition of cathepsin L by epoxysuccinyl peptides simultaneously addressing active-site and remote-site regions.
  Chembiochem, 9, 1721-1724.  
18184105 V.Hook, L.Funkelstein, D.Lu, S.Bark, J.Wegrzyn, and S.R.Hwang (2008).
Proteases for processing proneuropeptides into Peptide neurotransmitters and hormones.
  Annu Rev Pharmacol Toxicol, 48, 393-423.  
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.  
17298440 F.C.Reis, T.F.Costa, T.Sulea, A.Mezzetti, J.Scharfstein, D.Brömme, R.Ménard, and A.P.Lima (2007).
The propeptide of cruzipain--a potent selective inhibitor of the trypanosomal enzymes cruzipain and brucipain, and of the human enzyme cathepsin F.
  FEBS J, 274, 1224-1234.  
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.  
17919146 J.Zhang, J.M.Hamilton, D.R.Garrod, and C.Robinson (2007).
Interactions between mature Der p 1 and its free prodomain indicate membership of a new family of C1 peptidases.
  Allergy, 62, 1302-1309.  
17016456 B.P.Eckelman, G.S.Salvesen, and F.L.Scott (2006).
Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family.
  EMBO Rep, 7, 988-994.  
17075137 G.Kaulmann, G.J.Palm, K.Schilling, R.Hilgenfeld, and B.Wiederanders (2006).
The crystal structure of a Cys25 -> Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions.
  Protein Sci, 15, 2619-2629.
PDB code: 2c0y
16181340 L.C.Hsing, and A.Y.Rudensky (2005).
The lysosomal cysteine proteases in MHC class II antigen presentation.
  Immunol Rev, 207, 229-241.  
16045611 T.F.Kagawa, P.W.O'toole, and J.C.Cooney (2005).
SpeB-Spi: a novel protease-inhibitor pair from Streptococcus pyogenes.
  Mol Microbiol, 57, 650-666.  
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.  
15099520 B.Goulet, A.Baruch, N.S.Moon, M.Poirier, L.L.Sansregret, A.Erickson, M.Bogyo, and A.Nepveu (2004).
A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor.
  Mol Cell, 14, 207-219.  
15056364 C.Deraison, I.Darboux, L.Duportets, T.Gorojankina, Y.Rahbé, and L.Jouanin (2004).
Cloning and characterization of a gut-specific cathepsin L from the aphid Aphis gossypii.
  Insect Mol Biol, 13, 165-177.  
14585834 D.H.Ebert, S.A.Kopecky-Bromberg, and T.S.Dermody (2004).
Cathepsin B Is Inhibited in Mutant Cells Selected during Persistent Reovirus Infection.
  J Biol Chem, 279, 3837-3851.  
15606813 J.E.Ahn, R.A.Salzman, S.C.Braunagel, H.Koiwa, and K.Zhu-Salzman (2004).
Functional roles of specific bruchid protease isoforms in adaptation to a soybean protease inhibitor.
  Insect Mol Biol, 13, 649-657.  
14625277 K.C.Pandey, P.S.Sijwali, A.Singh, B.K.Na, and P.J.Rosenthal (2004).
Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2.
  J Biol Chem, 279, 3484-3491.  
14735489 M.Fabra, and J.Cerdà (2004).
Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation.
  Mol Reprod Dev, 67, 282-294.  
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.  
12534546 C.Mora, I.Flores, F.Montealegre, and A.Díaz (2003).
Cloning and expression of Blo t 1, a novel allergen from the dust mite Blomia tropicalis, homologous to cysteine proteases.
  Clin Exp Allergy, 33, 28-34.  
12887050 D.K.Nägler, and R.Ménard (2003).
Family C1 cysteine proteases: biological diversity or redundancy?
  Biol Chem, 384, 837-843.  
12860980 D.N.Li, S.P.Matthews, A.N.Antoniou, D.Mazzeo, and C.Watts (2003).
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
  J Biol Chem, 278, 38980-38990.  
12554931 D.Turk, and G.Guncar (2003).
Lysosomal cysteine proteases (cathepsins): promising drug targets.
  Acta Crystallogr D Biol Crystallogr, 59, 203-213.  
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.  
12874290 R.Filipek, M.Rzychon, A.Oleksy, M.Gruca, A.Dubin, J.Potempa, and M.Bochtler (2003).
The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease.
  J Biol Chem, 278, 40959-40966.
PDB code: 1pxv
12417635 E.Fiebiger, R.Maehr, J.Villadangos, E.Weber, A.Erickson, E.Bikoff, H.L.Ploegh, and A.M.Lennon-Duménil (2002).
Invariant chain controls the activity of extracellular cathepsin L.
  J Exp Med, 196, 1263-1269.  
12081494 F.Lecaille, Y.Choe, W.Brandt, Z.Li, C.S.Craik, and D.Brömme (2002).
Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity.
  Biochemistry, 41, 8447-8454.  
12108538 G.Lalmanach, A.Boulangé, C.Serveau, F.Lecaille, J.Scharfstein, F.Gauthier, and E.Authié (2002).
Congopain from Trypanosoma congolense: drug target and vaccine candidate.
  Biol Chem, 383, 739-749.  
12437108 M.Cappetta, I.Roth, A.Díaz, J.Tort, and L.Roche (2002).
Role of the prosegment of Fasciola hepatica cathepsin L1 in folding of the catalytic domain.
  Biol Chem, 383, 1215-1221.  
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.  
12553729 M.Kihara, H.Kakegawa, Y.Matano, E.Murata, H.Tsuge, H.Kido, and N.Katunuma (2002).
Chondroitin sulfate proteoglycan is a potent enhancer in the processing of procathepsin L.
  Biol Chem, 383, 1925-1929.  
12437139 S.Pietschmann, M.Fehn, G.Kaulmann, I.Wenz, B.Wiederanders, and K.Schilling (2002).
Foldase function of the cathepsin S proregion is strictly based upon its domain structure.
  Biol Chem, 383, 1453-1458.  
11483509 A.M.Lennon-Duménil, R.A.Roberts, K.Valentijn, C.Driessen, H.S.Overkleeft, A.Erickson, P.J.Peters, E.Bikoff, H.L.Ploegh, and P.Wolf Bryant (2001).
The p41 isoform of invariant chain is a chaperone for cathepsin L.
  EMBO J, 20, 4055-4064.  
11322895 F.Lecaille, E.Authié, T.Moreau, C.Serveau, F.Gauthier, and G.Lalmanach (2001).
Subsite specificity of trypanosomal cathepsin L-like cysteine proteases. Probing the S2 pocket with phenylalanine-derived amino acids.
  Eur J Biochem, 268, 2733-2741.  
11517942 K.Schilling, S.Pietschmann, M.Fehn, I.Wenz, and B.Wiederanders (2001).
Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion.
  Biol Chem, 382, 859-865.  
10931191 A.Brinker, E.Weber, D.Stoll, J.Voigt, A.Müller, N.Sewald, G.Jung, K.H.Wiesmüller, and P.Bohley (2000).
Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections.
  Eur J Biochem, 267, 5085-5092.  
10998237 C.E.Carter, H.Marriage, and P.W.Goodenough (2000).
Mutagenesis and kinetic studies of a plant cysteine proteinase with an unusual arrangement of acidic amino acids in and around the active site.
  Biochemistry, 39, 11005-11013.  
10852705 C.Luke, C.Schick, C.Tsu, J.C.Whisstock, J.A.Irving, D.Brömme, L.Juliano, G.P.Shi, H.A.Chapman, and G.A.Silverman (2000).
Simple modifications of the serpin reactive site loop convert SCCA2 into a cysteine proteinase inhibitor: a critical role for the P3' proline in facilitating RSL cleavage.
  Biochemistry, 39, 7081-7091.  
11048948 D.Greenbaum, K.F.Medzihradszky, A.Burlingame, and M.Bogyo (2000).
Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools.
  Chem Biol, 7, 569-581.  
11012686 J.Guay, J.P.Falgueyret, A.Ducret, M.D.Percival, and J.A.Mancini (2000).
Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides.
  Eur J Biochem, 267, 6311-6318.  
11027133 J.R.Somoza, H.Zhan, K.K.Bowman, L.Yu, K.D.Mortara, J.T.Palmer, J.M.Clark, and M.E.McGrath (2000).
Crystal structure of human cathepsin V.
  Biochemistry, 39, 12543-12551.
PDB code: 1fh0
10760593 K.Sol-Church, J.Frenck, and R.W.Mason (2000).
Mouse cathepsin M, a placenta-specific lysosomal cysteine protease related to cathepsins L and P.
  Biochim Biophys Acta, 1491, 289-294.  
  11206078 P.M.Smooker, J.C.Whisstock, J.A.Irving, S.Siyaguna, T.W.Spithill, and R.N.Pike (2000).
A single amino acid substitution affects substrate specificity in cysteine proteinases from Fasciola hepatica.
  Protein Sci, 9, 2567-2572.  
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.  
10679409 R.J.Riese, and H.A.Chapman (2000).
Cathepsins and compartmentalization in antigen presentation.
  Curr Opin Immunol, 12, 107-113.  
10806395 S.Kreusch, M.Fehn, G.Maubach, K.Nissler, W.Rommerskirch, K.Schilling, E.Weber, I.Wenz, and B.Wiederanders (2000).
An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases.
  Eur J Biochem, 267, 2965-2972.  
10681429 T.F.Kagawa, J.C.Cooney, H.M.Baker, S.McSweeney, M.Liu, S.Gubba, J.M.Musser, and E.N.Baker (2000).
Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: an integrin-binding cysteine protease.
  Proc Natl Acad Sci U S A, 97, 2235-2240.
PDB code: 1dki
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.  
10755997 X.Que, and S.L.Reed (2000).
Cysteine proteinases and the pathogenesis of amebiasis.
  Clin Microbiol Rev, 13, 196-206.  
10500110 A.R.Khan, N.Khazanovich-Bernstein, E.M.Bergmann, and M.N.James (1999).
Structural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursors.
  Proc Natl Acad Sci U S A, 96, 10968-10975.  
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.  
10092883 B.Turk, I.Dolenc, B.Lenarcic, I.Krizaj, V.Turk, J.G.Bieth, and I.Björk (1999).
Acidic pH as a physiological regulator of human cathepsin L activity.
  Eur J Biochem, 259, 926-932.  
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.  
10601010 C.M.Hosfield, J.S.Elce, P.L.Davies, and Z.Jia (1999).
Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation.
  EMBO J, 18, 6880-6889.
PDB code: 1df0
10029531 D.Brömme, Z.Li, M.Barnes, and E.Mehler (1999).
Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization.
  Biochemistry, 38, 2377-2385.  
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
10318784 I.Santamaría, G.Velasco, A.M.Pendás, A.Paz, and C.López-Otín (1999).
Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain.
  J Biol Chem, 274, 13800-13809.  
10347181 J.A.Huete-Pérez, J.C.Engel, L.S.Brinen, J.C.Mottram, and J.H.McKerrow (1999).
Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif.
  J Biol Chem, 274, 16249-16256.  
10373004 J.C.Whisstock, J.A.Irving, S.P.Bottomley, R.N.Pike, and A.M.Lesk (1999).
Serpins in the Caenorhabditis elegans genome.
  Proteins, 36, 31-41.  
10329692 J.Herold, S.G.Siddell, and A.E.Gorbalenya (1999).
A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold .
  J Biol Chem, 274, 14918-14925.  
9893980 J.M.LaLonde, B.Zhao, C.A.Janson, K.J.D'Alessio, M.S.McQueney, M.J.Orsini, C.M.Debouck, and W.W.Smith (1999).
The crystal structure of human procathepsin K.
  Biochemistry, 38, 862-869.
PDB code: 1by8
  10048321 J.Sivaraman, M.Lalumière, R.Ménard, and M.Cygler (1999).
Crystal structure of wild-type human procathepsin K.
  Protein Sci, 8, 283-290.
PDB code: 7pck
10410800 M.E.McGrath (1999).
The lysosomal cysteine proteases.
  Annu Rev Biophys Biomol Struct, 28, 181-204.  
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.
  Biochemistry, 38, 5017-5023.  
10447692 T.Okamoto, A.Yuki, N.Mitsuhashi, T.Minamikawa, and T.Mimamikawa (1999).
Asparaginyl endopeptidase (VmPE-1) and autocatalytic processing synergistically activate the vacuolar cysteine proteinase (SH-EP).
  Eur J Biochem, 264, 223-232.  
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.
  J Biol Chem, 274, 11390-11398.  
10074491 W.S.Hou, D.Brömme, Y.Zhao, E.Mehler, C.Dushey, H.Weinstein, C.S.Miranda, C.Fraga, F.Greig, J.Carey, D.L.Rimoin, R.J.Desnick, and B.D.Gelb (1999).
Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis.
  J Clin Invest, 103, 731-738.  
  10456870 Y.V.Matsuka, S.Pillai, S.Gubba, J.M.Musser, and S.B.Olmsted (1999).
Fibrinogen cleavage by the Streptococcus pyogenes extracellular cysteine protease and generation of antibodies that inhibit enzyme proteolytic activity.
  Infect Immun, 67, 4326-4333.  
9857201 A.Guarné, J.Tormo, R.Kirchweger, D.Pfistermueller, I.Fita, and T.Skern (1998).
Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition.
  EMBO J, 17, 7469-7479.
PDB code: 1qol
  9568890 A.R.Khan, and M.N.James (1998).
Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
  Protein Sci, 7, 815-836.  
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.
  Structure, 6, 51-61.
PDB code: 8pch
9737969 G.Lalmanach, F.Lecaille, J.R.Chagas, E.Authié, J.Scharfstein, M.A.Juliano, and F.Gauthier (1998).
Inhibition of trypanosomal cysteine proteinases by their propeptides.
  J Biol Chem, 273, 25112-25116.  
9523118 H.A.Chapman (1998).
Endosomal proteolysis and MHC class II function.
  Curr Opin Immunol, 10, 93.  
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.
  J Biol Chem, 273, 16816-16823.  
9694859 J.W.Cuozzo, K.Tao, M.Cygler, J.S.Mort, and G.G.Sahagian (1998).
Lysine-based structure responsible for selective mannose phosphorylation of cathepsin D and cathepsin L defines a common structural motif for lysosomal enzyme targeting.
  J Biol Chem, 273, 21067-21076.  
9600948 K.Shimizu, J.Cha, G.D.Stucky, and D.E.Morse (1998).
Silicatein alpha: cathepsin L-like protein in sponge biosilica.
  Proc Natl Acad Sci U S A, 95, 6234-6238.  
  9655332 M.E.McGrath, J.T.Palmer, D.Brömme, and J.R.Somoza (1998).
Crystal structure of human cathepsin S.
  Protein Sci, 7, 1294-1302.  
9624139 P.J.Wolters, W.W.Raymond, J.L.Blount, and G.H.Caughey (1998).
Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I.
  J Biol Chem, 273, 15514-15520.  
  9571245 R.G.Lingeman, D.S.Joy, M.A.Sherman, and S.E.Kane (1998).
Effect of carbohydrate position on lysosomal transport of procathepsin L.
  Mol Biol Cell, 9, 1135-1147.  
9565563 R.Jerala, E.Zerovnik, J.Kidric, and V.Turk (1998).
pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation.
  J Biol Chem, 273, 11498-11504.  
9468501 R.Ménard, E.Carmona, S.Takebe, E.Dufour, C.Plouffe, P.Mason, and J.S.Mort (1998).
Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro.
  J Biol Chem, 273, 4478-4484.  
9406551 A.R.Khan, M.M.Cherney, N.I.Tarasova, and M.N.James (1997).
Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin.
  Nat Struct Biol, 4, 1010-1015.
PDB code: 1avf
  9153250 B.Lenarcic, A.Ritonja, B.Strukelj, B.Turk, and V.Turk (1997).
Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain.
  J Biol Chem, 272, 13899-13903.  
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.
  Nat Struct Biol, 4, 109-111.
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.
  J Biol Chem, 272, 1197-1202.  
  9098904 C.J.Linnevers, M.E.McGrath, R.Armstrong, F.R.Mistry, M.G.Barnes, J.L.Klaus, J.T.Palmer, B.A.Katz, and D.Brömme (1997).
Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex.
  Protein Sci, 6, 919-921.  
9461297 G.Maubach, K.Schilling, W.Rommerskirch, I.Wenz, J.E.Schultz, E.Weber, and B.Wiederanders (1997).
The inhibition of cathepsin S by its propeptide--specificity and mechanism of action.
  Eur J Biochem, 250, 745-750.  
9033587 M.E.McGrath, J.L.Klaus, M.G.Barnes, and D.Brömme (1997).
Crystal structure of human cathepsin K complexed with a potent inhibitor.
  Nat Struct Biol, 4, 105-109.
PDB code: 1mem
9362483 R.Tikkanen, M.Peltola, C.Oinonen, J.Rouvinen, and L.Peltonen (1997).
Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase.
  EMBO J, 16, 6684-6693.  
9233788 S.C.Johnston, C.N.Larsen, W.J.Cook, K.D.Wilkinson, and C.P.Hill (1997).
Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution.
  EMBO J, 16, 3787-3796.
PDB code: 1uch
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