1su3: Difference between revisions

Revision as of 12:46, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1su3.png

Template:STRUCTURE 1su3

X-ray structure of human proMMP-1: New insights into collagenase actionX-ray structure of human proMMP-1: New insights into collagenase action

Template:ABSTRACT PUBMED 15611040

About this StructureAbout this Structure

1SU3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding., Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K, J Biol Chem. 2005 Mar 11;280(10):9578-85. Epub 2004 Dec 15. PMID:15611040

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''X-ray structure of human proMMP-1: New insights into collagenase action'''
+===X-ray structure of human proMMP-1: New insights into collagenase action===
-==Overview==
+<!--
-Vertebrate collagenases, members of the matrix metalloproteinase (MMP) family, initiate interstitial fibrillar collagen breakdown. It is essential in many biological processes, and unbalanced collagenolysis is associated with diseases such as arthritis, cancer, atherosclerosis, aneurysm, and fibrosis. These metalloproteinases are secreted from the cell as inactive precursors, procollagenases (proMMPs). To gain insights into the structural basis of their activation mechanisms and collagen binding, we have crystallized recombinant human proMMP-1 and determined its structure to 2.2 A resolution. The catalytic metalloproteinase domain and the C-terminal hemopexin (Hpx) domain show the classical MMP-fold, but the structure has revealed new features in surface loops and domain interaction. The prodomain is formed by a three-helix bundle and gives insight into the stepwise activation mechanism of proMMP-1. The prodomain interacts with the Hpx domain, which affects the position of the Hpx domain relative to the catalytic domain. This interaction results in a "closed" configuration of proMMP-1 in contrast to the "open" configuration observed previously for the structure of active MMP-1. This is the first evidence of mobility of the Hpx domain in relation to the catalytic domain, providing an important clue toward the understanding of the collagenase-collagen interaction and subsequent collagenolysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_15611040}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15611040}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Structural proteomics in europe]]
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