456c

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(New page: 200px<br /> <applet load="456c" size="450" color="white" frame="true" align="right" spinBox="true" caption="456c, resolution 2.4&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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<applet load="456c" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="456c, resolution 2.4&Aring;" />
caption="456c, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF COLLAGENASE-3 (MMP-13) COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID'''<br />
'''CRYSTAL STRUCTURE OF COLLAGENASE-3 (MMP-13) COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID'''<br />
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==About this Structure==
==About this Structure==
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456C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, CA and CBP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=456C OCA].
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456C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CBP:'>CBP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=456C OCA].
==Reference==
==Reference==
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[[Category: matrix metalloprotease]]
[[Category: matrix metalloprotease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:50:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:44:39 2008''

Revision as of 15:44, 15 February 2008


456c, resolution 2.4Å

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CRYSTAL STRUCTURE OF COLLAGENASE-3 (MMP-13) COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID

Overview

The X-ray crystal structures of the catalytic domain of human, collagenase-3 (MMP-13) and collagenase-1 (MMP-1) with bound inhibitors, provides a basis for understanding the selectivity profile of a novel, series of matrix metalloprotease (MMP) inhibitors. Differences in the, relative size and shape of the MMP S1' pockets suggest that this pocket is, a critical determinant of MMP inhibitor selectivity. The collagenase-3 S1', pocket is long and open, easily accommodating large P1' groups, such as, diphenylether. In contrast, the collagenase-1 S1' pocket must undergo a, conformational change to accommodate comparable P1' groups. The, selectivity of the diphenylether series of inhibitors for collagenase-3 is, largely determined by their affinity for the preformed S1' pocket of, collagenase-3, as compared to the induced fit in collagenase-1.

About this Structure

456C is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors., Lovejoy B, Welch AR, Carr S, Luong C, Broka C, Hendricks RT, Campbell JA, Walker KA, Martin R, Van Wart H, Browner MF, Nat Struct Biol. 1999 Mar;6(3):217-21. PMID:10074939

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