2cki

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Image:2cki.gif

2cki, resolution 1.70Å

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STRUCTURE OF ULILYSIN, A MEMBER OF THE PAPPALYSIN FAMILY OF METZINCIN METALLOENDOPEPTIDASES.

Overview

The metzincin clan encompasses several families of zinc-dependent, metalloproteases with proven function both in physiology and pathology., They act either as broad spectrum protein degraders or as sheddases, operating through limited proteolysis. Among the structurally, uncharacterized metzincin families are the pappalysins, of which the most, thoroughly studied member is human pregnancy-associated plasma protein A, (PAPP-A), a heavily glycosylated 170-kDa multidomain protein specifically, cleaving insulin-like growth factor (IGF)-binding proteins (IGFBPs)., Proulilysin is a 38-kDa archaeal protein that shares sequence similarity, with PAPP-A but encompasses only the pro-domain and the catalytic domain., It undergoes calcium-mediated autolytic activation, and the mature protein, adopts a ... [(full description)]

About this Structure

2CKI is a [Single protein] structure of sequence from [Methanosarcina acetivorans] with CA, ZN, ARG and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases., Tallant C, Garcia-Castellanos R, Seco J, Baumann U, Gomis-Ruth FX, J Biol Chem. 2006 Jun 30;281(26):17920-8. Epub 2006 Apr 20. PMID:16627477

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