830c: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:830c.gif|left|200px]] | [[Image:830c.gif|left|200px]] | ||
'''COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID''' | {{Structure | ||
|PDB= 830c |SIZE=350|CAPTION= <scene name='initialview01'>830c</scene>, resolution 1.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=RS1:4-[4-(4-CHLORO-PHENOXY)-BENZENESULFONYLMETHYL]-TETRAHYDRO-PYRAN-4-CARBOXYLIC ACID HYDROXYAMIDE'>RS1</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
830C is a [ | 830C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=830C OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10074939 10074939] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 29: | Line 38: | ||
[[Category: matrix metalloprotease]] | [[Category: matrix metalloprotease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:15:12 2008'' | ||
Revision as of 17:15, 20 March 2008
| |||||||||||||
| 830c, resolution 1.6Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | ZN, CA and RS1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
COLLAGENASE-3 (MMP-13) COMPLEXED TO A 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
830C is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Thu Mar 20 19:15:12 2008
