PDBsum entry: 1m6d

Hydrolase

PDB id: 1m6d

Contents

Protein chains

214 a.a. *

Ligands

MYP-MYP

MYP

Waters ×280

* Residue conservation analysis

PDB id:

1m6d

Name:

Hydrolase

Title:

Crystal structure of human cathepsin f

Structure:

Cathepsin f. Chain: a, b. Synonym: catsf. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: catf. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

Resolution:

1.70Å R-factor: 0.198 R-free: 0.222

Authors:

J.R.Somoza,J.T.Palmer,J.D.Ho

Key ref:

J.R.Somoza et al. (2002). The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators. J Mol Biol, 322, 559-568. PubMed id: 12225749 DOI: 10.1016/S0022-2836(02)00780-5

Date:

15-Jul-02 Release date: 15-Jul-03

Protein chains

Q9UBX1  (CATF_HUMAN) -  Cathepsin F

Seq: 484 a.a.

Struc: 214 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.22.41 - Cathepsin F.
• Reaction: The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (k(cat)/K(m)) comparable to that of cathepsin L.

 Gene Ontology (GO) functional annotation 

• Biological process: proteolysis (1 term)
• Biochemical function: cysteine-type peptidase activity (2 terms)

DOI no: 10.1016/S0022-2836(02)00780-5

J Mol Biol 322:559-568 (2002)

PubMed id: 12225749

The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators.

J.R.Somoza, J.T.Palmer, J.D.Ho.

ABSTRACT

Cathepsin F is a lysosomal cysteine protease of the papain family, and likely plays a regulatory role in processing the invariant chain that is associated with the major histocompatibility complex (MHC) class II. Evidence suggests that inhibiting cathepsin F activity will block MHC class II processing in macrophages. Consequently, inhibitors of this enzyme may be useful in treating certain diseases that involve an inappropriate or excessive immune response. We have determined the 1.7A structure of the mature domain of human cathepsin F associated with an irreversible vinyl sulfone inhibitor. This structure provides a basis for understanding cathepsin F's substrate specificity, and suggests ways of identifying potent and selective inhibitors of this enzyme.

Selected figure(s)

Figure 3.
Figure 3. Superposition of the active sites of molecules A (cyan) and B (red) that form the asymmetric unit.

Figure 4.
Figure 4. (a) A view of human cathepsin F, with arrows representing b-strands and with coils representing a-helices. (b) Solvent-accessible surface of human cathepsin F in approximately the same orientation.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 322, 559-568) copyright 2002.

Figures were selected by an automated process.