456c: Difference between revisions

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[[Image:456c.~~jpg~~|left|200px]]

[[Image:456c.png|left|200px]]

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

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

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10074939}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10074939 is the PubMed ID number.

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==About this Structure==

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[[Category: Hydrolase]]

[[Category: Matrix metalloprotease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ 4 22:~~18:40~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:22:08 2008''

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-[[Image:456c.jpg|left|200px]]
+{{Seed}}
+[[Image:456c.png|left|200px]]
 <!--
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 {{STRUCTURE_456c|  PDB=456c  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF COLLAGENASE-3 (MMP-13) COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10074939}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10074939 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10074939}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Hydrolase]]
 [[Category: Matrix metalloprotease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:18:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:22:08 2008''