1k3b: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_1k3b| PDB=1k3b | SCENE= }} | {{STRUCTURE_1k3b| PDB=1k3b | SCENE= }} | ||
===Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C): Exclusion Domain Added to an Endopeptidase Framework Creates the Machine for Activation of Granular Serine Proteases=== | |||
{{ABSTRACT_PUBMED_11726493}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:[http://omim.org/entry/245000 245000]]; also known as keratosis palmoplantaris with periodontopathia. PLS is an autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.<ref>PMID:11180601</ref><ref>PMID:12809647</ref><ref>PMID:10581027</ref><ref>PMID:10662808</ref><ref>PMID:11106356</ref><ref>PMID:11180012</ref><ref>PMID:11886537</ref><ref>PMID:11158173</ref><ref>PMID:12112662</ref><ref>PMID:14974080</ref><ref>PMID:15108292</ref><ref>PMID:15991336</ref> Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:[http://omim.org/entry/245010 245010]]; also known as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.<ref>PMID:10662807</ref> Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:[http://omim.org/entry/170650 170650]]; also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP). AP1 is characterized by severe and protracted gingival infections, leading to tooth loss. AP1 inheritance is autosomal dominant.<ref>PMID:10662808</ref><ref>PMID:14974080</ref> | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/CATC_HUMAN CATC_HUMAN]] Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.<ref>PMID:1586157</ref> | |||
==About this Structure== | ==About this Structure== | ||
| Line 14: | Line 16: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:011726493</ref><references group="xtra"/> | <ref group="xtra">PMID:011726493</ref><references group="xtra"/><references/> | ||
[[Category: Dipeptidyl-peptidase I]] | [[Category: Dipeptidyl-peptidase I]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||