This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1rtg

From Proteopedia

Revision as of 04:53, 3 May 2008 by OCA (Talk | contribs)
Jump to: navigation, search

Template:STRUCTURE 1rtg

C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2


Overview

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.

About this Structure

1RTG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function., Gohlke U, Gomis-Ruth FX, Crabbe T, Murphy G, Docherty AJ, Bode W, FEBS Lett. 1996 Jan 8;378(2):126-30. PMID:8549817 Page seeded by OCA on Sat May 3 07:53:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools