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Hydrolase/hydrolase inhibitor PDB id
1fh0
Jmol
Contents
Protein chains
221 a.a. *
Ligands
0IW ×2
SO4
Waters ×287
* Residue conservation analysis
PDB id:
1fh0
Name: Hydrolase/hydrolase inhibitor
Title: Crystal structure of human cathepsin v complexed with an irr vinyl sulfone inhibitor
Structure: Cathepsin v. Chain: a, b. Synonym: cathepsin l2. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
Resolution:
1.60Å     R-factor:   0.198     R-free:   0.211
Authors: J.R.Somoza
Key ref:
J.R.Somoza et al. (2000). Crystal structure of human cathepsin V. Biochemistry, 39, 12543-12551. PubMed id: 11027133 DOI: 10.1021/bi000951p
Date:
30-Jul-00     Release date:   30-Jul-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O60911  (CATL2_HUMAN) -  Cathepsin L2
Seq:
Struc: 		334 a.a.
221 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.43  - Cathepsin V.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     cysteine-type peptidase activity     2 terms  

 

 
DOI no: 10.1021/bi000951p Biochemistry 39:12543-12551 (2000)
PubMed id: 11027133  
 
 
Crystal structure of human cathepsin V.
J.R.Somoza, H.Zhan, K.K.Bowman, L.Yu, K.D.Mortara, J.T.Palmer, J.M.Clark, M.E.McGrath.
 
  ABSTRACT  
 
Cathepsin V is a lysosomal cysteine protease that is expressed in the thymus, testis and corneal epithelium. We have determined the 1.6 A resolution crystal structure of human cathepsin V associated with an irreversible vinyl sulfone inhibitor. The fold of this enzyme is similar to the fold adopted by other members of the papain superfamily of cysteine proteases. This study provides a framework for understanding the structural basis for cathepsin V's activity and will aid in the design of inhibitors of this enzyme. A comparison of cathepsin V's active site with the active sites of related proteases revealed a number of differences, especially in the S2 and S3 subsites, that could be exploited in identifying specific cathepsin V inhibitors or in identifying inhibitors of other cysteine proteases that would be selective against cathepsin V.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21326229 M.A.Adams-Cioaba, J.C.Krupa, C.Xu, J.S.Mort, and J.Min (2011).
Structural basis for the recognition and cleavage of histone H3 by cathepsin L.
  Nat Commun, 2, 197.
PDB codes: 3iv2 3k24
19846555 M.Renko, J.Sabotic, M.Mihelic, J.Brzin, J.Kos, and D.Turk (2010).
Versatile loops in mycocypins inhibit three protease families.
  J Biol Chem, 285, 308-316.
PDB codes: 3h6q 3h6r 3h6s
18362148 M.Mihelic, A.Dobersek, G.Guncar, and D.Turk (2008).
Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation.
  J Biol Chem, 283, 14453-14460.  
17923478 P.C.Ong, S.McGowan, M.C.Pearce, J.A.Irving, W.T.Kan, S.A.Grigoryev, B.Turk, G.A.Silverman, K.Brix, S.P.Bottomley, J.C.Whisstock, and R.N.Pike (2007).
DNA accelerates the inhibition of human cathepsin v by serpins.
  J Biol Chem, 282, 36980-36986.  
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.  
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.  
  12401493 D.C.Greenbaum, W.D.Arnold, F.Lu, L.Hayrapetian, A.Baruch, J.Krumrine, S.Toba, K.Chehade, D.Brömme, I.D.Kuntz, and M.Bogyo (2002).
Small molecule affinity fingerprinting. A tool for enzyme family subclassification, target identification, and inhibitor design.
  Chem Biol, 9, 1085-1094.  
11371637 U.Ilangovan, H.Ton-That, J.Iwahara, O.Schneewind, and R.T.Clubb (2001).
Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus.
  Proc Natl Acad Sci U S A, 98, 6056-6061.
PDB code: 1ija
11257924 K.K.Jain (2000).
Applications of proteomics in oncology.
  Pharmacogenomics, 1, 385-393.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.