1rtg

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[[Image:1rtg.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1rtg| PDB=1rtg | SCENE= }}
{{STRUCTURE_1rtg| PDB=1rtg | SCENE= }}
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'''C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2'''
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===C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8549817 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8549817}}
==About this Structure==
==About this Structure==
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[[Category: Metalloprotease]]
[[Category: Metalloprotease]]
[[Category: Metzincin]]
[[Category: Metzincin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:53:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:12:01 2008''

Revision as of 01:12, 29 July 2008

Image:1rtg.png

Template:STRUCTURE 1rtg

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

Template:ABSTRACT PUBMED 8549817

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

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