Authors:
U Gohlke, FX Gomis-Rüth, T Crabbe, G Murphy, AJ Docherty, W Bode
Journal name: 
FEBS Lett
Citation info: 
378(2):126-130
Abstract: 
In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.
DOI: 
http://doi.org/10.1016/0014-5793(95)01435-7
E-pub date: 
31 Dec 1995
Users with this publication listed: 
Gillian Murphy