PDBsum entry 1cew

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Proteinase inhibitor(cysteine) PDB id
Protein chain
108 a.a. *
Waters ×123
* Residue conservation analysis
PDB id:
Name: Proteinase inhibitor(cysteine)
Title: The 2.0 angstroms x-ray crystal structure of chicken egg whi cystatin and its possible mode of interaction with cysteine proteinases
Structure: Cystatin. Chain: i. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: egg
2.00Å     R-factor:   0.198    
Authors: W.Bode,D.Musil,R.Huber
Key ref: W.Bode et al. (1988). The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J, 7, 2593-2599. PubMed id: 3191914
21-Apr-93     Release date:   31-Jan-94    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P01038  (CYT_CHICK) -  Cystatin
139 a.a.
108 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     negative regulation of peptidase activity   2 terms 
  Biochemical function     peptidase inhibitor activity     2 terms  


EMBO J 7:2593-2599 (1988)
PubMed id: 3191914  
The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.
W.Bode, R.Engh, D.Musil, U.Thiele, R.Huber, A.Karshikov, J.Brzin, J.Kos, V.Turk.
The crystal structure of chicken egg white cystatin has been solved by X-ray diffraction methods using the multiple isomorphous replacement technique. Its structure has been refined to a crystallographic R value of 0.19 using X-ray data between 6 and 2.0A. The molecule consists mainly of a straight five-turn alpha-helix, a five-stranded antiparallel beta-pleated sheet which is twisted and wrapped around the alpha-helix and an appending segment of partially alpha-helical geometry. The 'highly conserved' region from Gln53I to Gly57I implicated with binding to cysteine proteinases folds into a tight beta-hairpin loop which on opposite sides is flanked by the amino-terminal segment and by a second hairpin loop made up of the similarly conserved segment Pro103I - Trp104I. These loops and the amino-terminal Gly9I - Ala10I form a wedge-shaped 'edge' which is quite complementary to the 'active site cleft' of papain. Docking experiments suggest a unique model for the interaction of cystatin and papain: according to it both hairpin loops of cystatin make major binding interactions with the highly conserved residues Gly23, Gln19, Trp177 and Ala136 of papain in the neighbourhood of the reactive site Cys25; the amino-terminal segment Gly9I - Ala10I of bound cystatin is directed towards the substrate subsite S2, but in an inappropriate conformation and too far away to be attacked by the reactive site Cys25. As a consequence, the mechanism of the interaction between cysteine proteinases and their cystatin-like inhibitors seems to be fundamentally different from the 'standard mechanism' defined for serine proteinases and most of their protein inhibitors.

Literature references that cite this PDB file's key reference

  PubMed id Reference
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The crystal structures of two salivary cystatins from the tick Ixodes scapularis and the effect of these inhibitors on the establishment of Borrelia burgdorferi infection in a murine model.
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PDB codes: 3lh4 3li7 3mwz
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Stefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleft.
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PDB code: 3k9m
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Crystal structure of human cystatin C stabilized against amyloid formation.
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PDB code: 3gax
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PDB code: 3e1z
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Inactivation of the cystatin E/M tumor suppressor gene in cervical cancer.
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18702630 N.Kocevar, N.Obermajer, and S.Kreft (2008).
Membrane permeability of acylated cystatin depends on the fatty acyl chain length.
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18028412 T.Joensuu, A.E.Lehesjoki, and O.Kopra (2008).
Molecular background of EPM1-Unverricht-Lundborg disease.
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18605793 T.Y.Kim, K.Y.Han, E.H.Shin, and J.Y.Chai (2008).
Antigenic properties of cystatin-binding cysteine proteinases from Neodiplostomum seoulense.
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17617796 E.Wieczerzak, S.Rodziewicz-Motowidło, E.Jankowska, A.Giełdoń, and J.Ciarkowski (2007).
An enormously active and selective azapeptide inhibitor of cathepsin B.
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17698852 M.Kotsyfakis, S.Karim, J.F.Andersen, T.N.Mather, and J.M.Ribeiro (2007).
Selective cysteine protease inhibition contributes to blood-feeding success of the tick Ixodes scapularis.
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Two decades of thyroglobulin type-1 domain research.
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17470433 M.Wahlbom, X.Wang, V.Lindström, E.Carlemalm, M.Jaskolski, and A.Grubb (2007).
Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping.
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Improved acylation method enables efficient delivery of functional palmitoylated cystatin into epithelial cells.
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Identification of candidate angiogenic inhibitors processed by matrix metalloproteinase 2 (MMP-2) in cell-based proteomic screens: disruption of vascular endothelial growth factor (VEGF)/heparin affin regulatory peptide (pleiotrophin) and VEGF/Connective tissue growth factor angiogenic inhibitory complexes by MMP-2 proteolysis.
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PDB code: 2oul
17681235 T.Miyaji, Y.Kouzuma, J.Yaguchi, R.Matsumoto, M.R.Kanost, K.J.Kramer, and M.Yonekura (2007).
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Molecular dynamics simulations to investigate the domain swapping mechanism of human cystatin C.
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16965553 A.Kiggundu, M.C.Goulet, C.Goulet, J.F.Dubuc, D.Rivard, M.Benchabane, G.Pépin, C.van der Vyver, K.Kunert, and D.Michaud (2006).
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16601115 A.W.Schüttelkopf, G.Hamilton, C.Watts, and D.M.van Aalten (2006).
Structural basis of reduction-dependent activation of human cystatin F.
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PDB code: 2ch9
16407198 B.O.Smith, N.C.Picken, G.D.Westrop, K.Bromek, J.C.Mottram, and G.H.Coombs (2006).
The structure of Leishmania mexicana ICP provides evidence for convergent evolution of cysteine peptidase inhibitors.
  J Biol Chem, 281, 5821-5828.
PDB code: 2c34
16434741 J.He, Y.Song, N.Ueyama, A.Saito, H.Azakami, and A.Kato (2006).
Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site-specific glycosylation in yeast.
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16470583 J.M.Aguiar, O.L.Franco, D.J.Rigden, C.Bloch, A.C.Monteiro, V.M.Flores, T.Jacinto, J.Xavier-Filho, A.E.Oliveira, M.F.Grossi-de-Sá, and K.V.Fernandes (2006).
Molecular modeling and inhibitory activity of cowpea cystatin against bean bruchid pests.
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16446111 J.Messens, and J.F.Collet (2006).
Pathways of disulfide bond formation in Escherichia coli.
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17132111 L.Grunclová, M.Horn, M.Vancová, D.Sojka, Z.Franta, M.Mares, and P.Kopácek (2006).
Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity.
  Biol Chem, 387, 1635-1644.  
16698543 M.J.Bennett, M.R.Sawaya, and D.Eisenberg (2006).
Deposition diseases and 3D domain swapping.
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16864794 S.X.Wang, K.C.Pandey, J.R.Somoza, P.S.Sijwali, T.Kortemme, L.S.Brinen, R.J.Fletterick, P.J.Rosenthal, and J.H.McKerrow (2006).
Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease.
  Proc Natl Acad Sci U S A, 103, 11503-11508.
PDB code: 1yvb
15698574 A.Aagaard, P.Listwan, N.Cowieson, T.Huber, T.Ravasi, C.A.Wells, J.U.Flanagan, S.Kellie, D.A.Hume, B.Kobe, and J.L.Martin (2005).
An inflammatory role for the mammalian carboxypeptidase inhibitor latexin: relationship to cystatins and the tumor suppressor TIG1.
  Structure, 13, 309-317.
PDB code: 1wnh
15647900 A.H.Yang, and K.W.Yeh (2005).
Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1).
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15489503 D.A.Breustedt, I.P.Korndörfer, B.Redl, and A.Skerra (2005).
The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands.
  J Biol Chem, 280, 484-493.
PDB code: 1xki
16556043 D.Keppler, and F.Sierra (2005).
Role of cystatins in tumor neovascularization.
  Future Oncol, 1, 661-672.  
16014938 E.Espagne, V.Douris, G.Lalmanach, B.Provost, L.Cattolico, J.Lesobre, S.Kurata, K.Iatrou, J.M.Drezen, and E.Huguet (2005).
A virus essential for insect host-parasite interactions encodes cystatins.
  J Virol, 79, 9765-9776.  
16650055 E.Wieczerzak, E.Jankowska, S.Rodziewicz-Motowidło, A.Giełdoń, J.Lagiewka, Z.Grzonka, M.Abrahamson, A.Grubb, and D.Brömme (2005).
Novel azapeptide inhibitors of cathepsins B and K. Structural background to increased specificity for cathepsin B.
  J Pept Res, 66, 1.  
15775973 J.Otlewski, F.Jelen, M.Zakrzewska, and A.Oleksy (2005).
The many faces of protease-protein inhibitor interaction.
  EMBO J, 24, 1303-1310.  
16279937 J.T.Christeller (2005).
Evolutionary mechanisms acting on proteinase inhibitor variability.
  FEBS J, 272, 5710-5722.  
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
15906014 M.Brage, M.Abrahamson, V.Lindström, A.Grubb, and U.H.Lerner (2005).
Different cysteine proteinases involved in bone resorption and osteoclast formation.
  Calcif Tissue Int, 76, 439-447.  
16170782 R.Janowski, M.Kozak, M.Abrahamson, A.Grubb, and M.Jaskolski (2005).
3D domain-swapped human cystatin C with amyloidlike intermolecular beta-sheets.
  Proteins, 61, 570-578.
PDB code: 1tij
16080717 Y.C.Su, J.C.Lin, and H.L.Liu (2005).
Homology model and molecular dynamics simulation of carp ovum cystatin.
  Biotechnol Prog, 21, 1315-1320.  
15184683 B.Heras, M.A.Edeling, H.J.Schirra, S.Raina, and J.L.Martin (2004).
Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.
  Proc Natl Acad Sci U S A, 101, 8876-8881.
PDB codes: 1v57 1v58
15028721 M.Nilsson, X.Wang, S.Rodziewicz-Motowidlo, R.Janowski, V.Lindström, P.Onnerfjord, G.Westermark, Z.Grzonka, M.Jaskolski, and A.Grubb (2004).
Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C.
  J Biol Chem, 279, 24236-24245.  
15255188 M.S.El-Halawany, S.Ohkouchi, H.Shibata, K.Hitomi, and M.Maki (2004).
Identification of cysteine protease inhibitors that belong to cystatin family 1 in the cellular slime mold Dictyostelium discoideum.
  Biol Chem, 385, 547-550.  
15598351 S.Cheek, Y.Qi, S.S.Krishna, L.N.Kinch, and N.V.Grishin (2004).
4SCOPmap: automated assignment of protein structures to evolutionary superfamilies.
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12853462 A.E.Lehesjoki (2003).
Molecular background of progressive myoclonus epilepsy.
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12556469 A.Heiss, A.DuChesne, B.Denecke, J.Grötzinger, K.Yamamoto, T.Renné, and W.Jahnen-Dechent (2003).
Structural basis of calcification inhibition by alpha 2-HS glycoprotein/fetuin-A. Formation of colloidal calciprotein particles.
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14629266 A.Jasir, F.Kasprzykowski, R.Kasprzykowska, V.Lindström, C.Schalén, and A.Grubb (2003).
New antimicrobial cystatin C-based peptide active against gram-positive bacterial pathogens, including methicillin-resistant Staphylococcus aureus and multiresistant coagulase-negative staphylococci.
  APMIS, 111, 1004-1010.  
12787025 B.Belenghi, F.Acconcia, M.Trovato, M.Perazzolli, A.Bocedi, F.Polticelli, P.Ascenzi, and M.Delledonne (2003).
AtCYS1, a cystatin from Arabidopsis thaliana, suppresses hypersensitive cell death.
  Eur J Biochem, 270, 2593-2604.  
12887049 B.Turk, H.Fritz, and V.Turk (2003).
Vito Turk--30 years of research on cysteine proteases and their inhibitors.
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12871550 J.Katsunuma, T.Sugi, A.Inomo, H.Matsubayashi, S.I.Izumi, and T.Makino (2003).
Kininogen domain 3 contains regions recognized by antiphosphatidylethanolamine antibodies.
  J Thromb Haemost, 1, 132-138.  
12700194 Y.Li, P.J.Friel, D.J.McLean, and M.D.Griswold (2003).
Cystatin E1 and E2, new members of male reproductive tract subgroup within cystatin type 2 family.
  Biol Reprod, 69, 489-500.  
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.
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12142451 D.J.Rigden, V.V.Mosolov, and M.Y.Galperin (2002).
Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors.
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Overexpression and structural study of the cathelicidin motif of the protegrin-3 precursor.
  Biochemistry, 41, 21-30.  
12065604 J.Hong, K.Yoshida, and M.R.Rosner (2002).
Characterization of a cysteine proteinase inhibitor induced during neuronal cell differentiation.
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12437100 K.Hatano, Y.Sawano, and M.Tanokura (2002).
Structure-function relationship of bromelain isoinhibitors from pineapple stem.
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12234368 M.A.Arnaout (2002).
Integrin structure: new twists and turns in dynamic cell adhesion.
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Coming to grips with integrin binding to ligands.
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11918752 M.Mussap, M.Dalla Vestra, P.Fioretto, A.Saller, M.Varagnolo, R.Nosadini, and M.Plebani (2002).
Cystatin C is a more sensitive marker than creatinine for the estimation of GFR in type 2 diabetic patients.
  Kidney Int, 61, 1453-1461.  
12444065 Y.Li, P.J.Friel, M.O.Robinson, D.J.McLean, and M.D.Griswold (2002).
Identification and characterization of testis- and epididymis-specific genes: cystatin SC and cystatin TE-1.
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12021428 Y.Liu, and D.Eisenberg (2002).
3D domain swapping: as domains continue to swap.
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11448731 A.Ruzindana-Umunyana, and J.M.Weber (2001).
Interactions of human lacrimal and salivary cystatins with adenovirus endopeptidase.
  Antiviral Res, 51, 203-214.  
11301256 B.Manoury, W.F.Gregory, R.M.Maizels, and C.Watts (2001).
Bm-CPI-2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing.
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11154913 C.Watts (2001).
Antigen processing in the endocytic compartment.
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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.
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Phage display selection of hairpin loop soyacystatin variants that mediate high affinity inhibition of a cysteine proteinase.
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11299325 M.Calero, M.Pawlik, C.Soto, E.M.Castaño, E.M.Sigurdsson, A.Kumar, G.Gallo, B.Frangione, and E.Levy (2001).
Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type.
  J Neurochem, 77, 628-637.  
11727836 P.Wojnar, W.van't Hof, P.Merschak, M.Lechner, and B.Redl (2001).
The N-terminal part of recombinant human tear lipocalin/von Ebner's gland protein confers cysteine proteinase inhibition depending on the presence of the entire cystatin-like sequence motifs.
  Biol Chem, 382, 1515-1520.  
11687443 T.Y.Kim, S.Y.Kang, S.H.Park, K.Sukontason, K.Sukontason, and S.J.Hong (2001).
Cystatin capture enzyme-linked immunosorbent assay for serodiagnosis of human clonorchiasis and profile of captured antigenic protein of Clonorchis sinensis.
  Clin Diagn Lab Immunol, 8, 1076-1080.  
11101290 K.Nagata, N.Kudo, K.Abe, S.Arai, and M.Tanokura (2000).
Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica.
  Biochemistry, 39, 14753-14760.
PDB code: 1eqk
10823937 R.A.Staniforth, J.L.Dean, Q.Zhong, E.Zerovnik, A.R.Clarke, and J.P.Waltho (2000).
The major transition state in folding need not involve the immobilization of side chains.
  Proc Natl Acad Sci U S A, 97, 5790-5795.  
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Characterization of the interface structure of enzyme-inhibitor complex by using hydrogen-deuterium exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry.
  Protein Sci, 9, 2497-2505.  
  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.  
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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Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site.
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10531502 M.Kozak, E.Jankowska, R.Janowski, Z.Grzonka, A.Grubb, M.Alvarez Fernandez, M.Abrahamson, and M.Jaskolski (1999).
Expression of a selenomethionyl derivative and preliminary crystallographic studies of human cystatin C.
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10353845 S.Estrada, A.Pavlova, and I.Björk (1999).
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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9521728 A.Hall, I.Ekiel, R.W.Mason, F.Kasprzykowski, A.Grubb, and M.Abrahamson (1998).
Structural basis for different inhibitory specificities of human cystatins C and D.
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  9568890 A.R.Khan, and M.N.James (1998).
Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
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9860845 B.Gerhartz, I.Ekiel, and M.Abrahamson (1998).
Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C.
  Biochemistry, 37, 17309-17317.  
  9865609 E.Lorbach, Z.Wang, and P.Dröge (1998).
RNA splicing of bacterial genes in eukaryotes.
  Biol Chem, 379, 1355-1358.  
9715907 E.Zerovnik, R.Jerala, R.Virden, L.Kroon Zitko, V.Turk, and J.P.Waltho (1998).
On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate states.
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9687368 I.R.Vetter, M.W.Parker, A.D.Tucker, J.H.Lakey, F.Pattus, and D.Tsernoglou (1998).
Crystal structure of a colicin N fragment suggests a model for toxicity.
  Structure, 6, 863-874.
PDB code: 1a87
9733783 J.Ni, M.A.Fernandez, L.Danielsson, R.A.Chillakuru, J.Zhang, A.Grubb, J.Su, R.Gentz, and M.Abrahamson (1998).
Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor.
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9877092 M.Mussap, N.Ruzzante, M.Varagnolo, and M.Plebani (1998).
Quantitative automated particle-enhanced immunonephelometric assay for the routinary measurement of human cystatin C.
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  9524060 M.T.Stubbs, M.Renatus, and W.Bode (1998).
An active zymogen: unravelling the mystery of tissue-type plasminogen activator.
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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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9632704 S.Halfon, J.Ford, J.Foster, L.Dowling, L.Lucian, M.Sterling, Y.Xu, M.Weiss, M.Ikeda, D.Liggett, A.Helms, C.Caux, S.Lebecque, C.Hannum, S.Menon, T.McClanahan, D.Gorman, and G.Zurawski (1998).
Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cells.
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9826679 V.Töhönen, C.Osterlund, and K.Nordqvist (1998).
Testatin: a cystatin-related gene expressed during early testis development.
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9447266 J.E.Bell, E.Cunningham, C.Belt, J.D.Featherstone, and J.Bell (1997).
Examination of the potential structure of human salivary cystatins based on computer modelling.
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9099741 J.Ni, M.Abrahamson, M.Zhang, M.A.Fernandez, A.Grubb, J.Su, G.L.Yu, Y.Li, D.Parmelee, L.Xing, T.A.Coleman, S.Gentz, R.Thotakura, N.Nguyen, M.Hesselberg, and R.Gentz (1997).
Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins.
  J Biol Chem, 272, 10853-10858.  
  9536278 M.Abrahamson, M.Wikström, J.Potempa, S.Renvert, and A.Hall (1997).
Modification of cystatin C activity by bacterial proteinases and neutrophil elastase in periodontitis.
  Mol Pathol, 50, 291-297.  
9063457 S.Peloille, A.Esnard, J.L.Dacheux, F.Guillou, F.Gauthier, and F.Esnard (1997).
Interactions between ovine cathepsin L, cystatin C and alpha 2-macroglobulin. Potential role in the genital tract.
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Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli.
  Protein Sci, 6, 2180-2187.  
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The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.
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Friends and relations of the cystatin superfamily--new members and their evolution.
  Protein Sci, 6, 5.  
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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8718861 I.Björk, I.Brieditis, E.Raub-Segall, E.Pol, K.Håkansson, and M.Abrahamson (1996).
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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8737928 I.Olafsson, L.Thorsteinsson, and O.Jensson (1996).
The molecular pathology of hereditary cystatin C amyloid angiopathy causing brain hemorrhage.
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8611527 K.Hatano, M.Kojima, M.Tanokura, and K.Takahashi (1996).
Solution structure of bromelain inhibitor IV from pineapple stem: structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from soybean.
  Biochemistry, 35, 5379-5384.
PDB codes: 1bi6 2bi6
8910420 L.Verdot, G.Lalmanach, V.Vercruysse, S.Hartmann, R.Lucius, J.Hoebeke, F.Gauthier, and B.Vray (1996).
Cystatins up-regulate nitric oxide release from interferon-gamma-activated mouse peritoneal macrophages.
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Characterization of cystatin C from bovine parotid glands: cysteine proteinase inhibition and antiviral properties.
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8870072 P.Bork, A.K.Downing, B.Kieffer, and I.D.Campbell (1996).
Structure and distribution of modules in extracellular proteins.
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8706679 P.Storici, A.Tossi, B.Lenarcic, and D.Romeo (1996).
Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides.
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8829807 Y.J.Tsai, G.D.Chang, C.J.Huang, Y.S.Chang, and F.L.Huang (1996).
Purification and molecular cloning of carp ovarian cystatin.
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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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The role of vascular permeability factor and basic fibroblast growth factor in tumor angiogenesis.
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7814406 B.Hu, L.Coulson, B.Moyer, and P.A.Price (1995).
Isolation and molecular cloning of a novel bone phosphoprotein related in sequence to the cystatin family of thiol protease inhibitors.
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  7626231 B.Turk, J.G.Bieth, I.Björk, I.Dolenc, D.Turk, N.Cimerman, J.Kos, A.Colic, V.Stoka, and V.Turk (1995).
Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins.
  Biol Chem Hoppe Seyler, 376, 225-230.  
  8528085 B.Turk, V.Stoka, I.Björk, C.Boudier, G.Johansson, I.Dolenc, A.Colic, J.G.Bieth, and V.Turk (1995).
High-affinity binding of two molecules of cysteine proteinases to low-molecular-weight kininogen.
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7671300 C.D.Mol, A.S.Arvai, R.J.Sanderson, G.Slupphaug, B.Kavli, H.E.Krokan, D.W.Mosbaugh, and J.A.Tainer (1995).
Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA.
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PDB code: 1ugh
7619504 G.A.Cornwall, and S.R.Hann (1995).
Transient appearance of CRES protein during spermatogenesis and caput epididymal sperm maturation.
  Mol Reprod Dev, 41, 37-46.  
8747425 G.Lalmanach, C.Serveau, M.Brillard-Bourdet, J.R.Chagas, R.Mayer, L.Juliano, and F.Gauthier (1995).
Conserved cystatin segments as models for designing specific substrates and inhibitors of cysteine proteinases.
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Primary structure, sequence-specific 1H-NMR assignments and secondary structure in solution of bromelain inhibitor VI from pineapple stem.
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7925354 E.A.Auerswald, D.K.Nägler, A.J.Schulze, R.A.Engh, G.Genenger, W.Machleidt, and H.Fritz (1994).
Production, inhibitory activity, folding and conformational analysis of an N-terminal and an internal deletion variant of chicken cystatin.
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Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinases.
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7925405 R.Jerala, L.Kroon-Zitko, T.Popovic, and V.Turk (1994).
Elongation on the amino-terminal part of stefin B decreases inhibition of cathepsin H.
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8427630 G.Lalmanach, J.Hoebeke, T.Moreau, M.Brillard-Bourdet, M.Ferrer-Ditt Martino, F.Borras-Cuesta, and F.Gauthier (1993).
Interaction between cystatin-derived peptides and papain.
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1587359 A.V.Kajava (1992).
Left-handed topology of super-secondary structure formed by aligned alpha-helix and beta-hairpin.
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Recombinant chicken egg white cystatin variants of the QLVSG region.
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1593134 G.Lalmanach, J.Hoebeke, T.Moreau, M.Ferrer-Di Martino, and F.Gauthier (1992).
An immunochemical approach to investigating the mechanism of inhibition of cysteine proteinases by members of the cystatin superfamily.
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1544477 I.Björk, and E.Pol (1992).
Biphasic transition curve on denaturation of chicken cystatin by guanidinium chloride. Evidence for an independently unfolding structural region.
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Structural organization of the gene encoding rat cystatin beta.
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1541261 W.Bode, and R.Huber (1992).
Natural protein proteinase inhibitors and their interaction with proteinases.
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Inactivation of human cystatin C and kininogen by human cathepsin D.
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  1868826 D.Musil, D.Zucic, D.Turk, R.A.Engh, I.Mayr, R.Huber, T.Popovic, V.Turk, T.Towatari, and N.Katunuma (1991).
The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.
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PDB code: 1huc
1879418 E.A.Auerswald, G.Genenger, R.Mentele, S.Lenzen, I.Assfalg-Machleidt, L.Mitschang, H.Oschkinat, and H.Fritz (1991).
Purification and characterization of a chicken egg white cystatin variant expressed in an Escherichia coli pIN-III-ompA system.
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1798057 M.J.Berg, and N.Marks (1991).
Brain cysteine proteinase inhibitors II: evidence that a 21-kDa papain-binding component resembles ras p21.
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1743294 R.Ishima, A.Tamura, K.Akasaka, K.Hamaguchi, K.Makino, T.Murachi, M.Hatanaka, and M.Maki (1991).
Structure of the active 27-residue fragment of human calpastatin.
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1855589 V.Turk, and W.Bode (1991).
The cystatins: protein inhibitors of cysteine proteinases.
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The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.
  EMBO J, 9, 1939-1947.
PDB code: 1stf
  2744786 H.Ishiguro, I.Ohkubo, M.Mizokami, K.Titani, and M.Sasaki (1989).
The use of monoclonal antibodies to define levels of cystatin C in normal human serum.
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2678630 T.E.Creighton, and N.J.Darby (1989).
Functional evolutionary divergence of proteolytic enzymes and their inhibitors.
  Trends Biochem Sci, 14, 319-324.  
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