1hfc
From Proteopedia
|
1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE
Contents |
Overview
The X-ray crystal structure of a 19 kDa active fragment of human, fibroblast collagenase has been determined by the multiple isomorphous, replacement method and refined at 1.56 A resolution to an R-factor of, 17.4%. The current structure includes a bound hydroxamate inhibitor, 88, waters and three metal atoms (two zincs and a calcium). The overall, topology of the enzyme, comprised of a five stranded beta-sheet and three, alpha-helices, is similar to the thermolysin-like metalloproteinases., There are some important differences between the collagenase and, thermolysin families of enzymes. The active site zinc ligands are all, histidines (His-218, His-222, and His-228). The presence of a second zinc, ion in a structural role is a unique feature of the matrix, metalloproteinases. The binding properties of the active site cleft are, more dependent on the main chain conformation of the enzyme (and, substrate) compared with thermolysin. A mechanism of action for peptide, cleavage similar to that of thermolysin is proposed for fibroblast, collagenase.
Disease
Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[120353]
About this Structure
1HFC is a Single protein structure of sequence from Homo sapiens with ZN, CA and PLH as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Full crystallographic information is available from OCA.
Reference
1.56 A structure of mature truncated human fibroblast collagenase., Spurlino JC, Smallwood AM, Carlton DD, Banks TM, Vavra KJ, Johnson JS, Cook ER, Falvo J, Wahl RC, Pulvino TA, et al., Proteins. 1994 Jun;19(2):98-109. PMID:8090713
Page seeded by OCA on Mon Nov 12 17:17:18 2007
