1rtg
From Proteopedia
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| , resolution 2.6Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Gelatinase A, with EC number 3.4.24.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:32:42 2008
