2d1n

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(New page: 200px<br /> <applet load="2d1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d1n, resolution 2.37&Aring;" /> '''Collagenase-3 (MMP-...)
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[[Image:2d1n.gif|left|200px]]<br />
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[[Image:2d1n.gif|left|200px]]<br /><applet load="2d1n" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2d1n" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2d1n, resolution 2.37&Aring;" />
caption="2d1n, resolution 2.37&Aring;" />
'''Collagenase-3 (MMP-13) complexed to a hydroxamic acid inhibitor'''<br />
'''Collagenase-3 (MMP-13) complexed to a hydroxamic acid inhibitor'''<br />
==Overview==
==Overview==
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Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3), and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453 have, been solved at 2.01 and 2.37A resolutions, respectively. The results, revealed that the binding modes for this inhibitor to MMP-3 and -13 were, quite similar. However, subtle comparative differences were observed at, the bottom of S1' pockets, which were occupied with the guanidinomethyl, moiety of the inhibitor. A remarkable feature of the inhibitor was the, deep penetration of its long aliphatic chain into the S1' pocket and, exposure of the guanidinomethyl moiety to the solvent.
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Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453 have been solved at 2.01 and 2.37A resolutions, respectively. The results revealed that the binding modes for this inhibitor to MMP-3 and -13 were quite similar. However, subtle comparative differences were observed at the bottom of S1' pockets, which were occupied with the guanidinomethyl moiety of the inhibitor. A remarkable feature of the inhibitor was the deep penetration of its long aliphatic chain into the S1' pocket and exposure of the guanidinomethyl moiety to the solvent.
==About this Structure==
==About this Structure==
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2D1N 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 FA4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D1N OCA].
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2D1N 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=FA4:'>FA4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1N OCA].
==Reference==
==Reference==
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[[Category: hydorolase metalloprotease]]
[[Category: hydorolase metalloprotease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:25:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:27 2008''

Revision as of 14:54, 21 February 2008


2d1n, resolution 2.37Å

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Collagenase-3 (MMP-13) complexed to a hydroxamic acid inhibitor

Overview

Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453 have been solved at 2.01 and 2.37A resolutions, respectively. The results revealed that the binding modes for this inhibitor to MMP-3 and -13 were quite similar. However, subtle comparative differences were observed at the bottom of S1' pockets, which were occupied with the guanidinomethyl moiety of the inhibitor. A remarkable feature of the inhibitor was the deep penetration of its long aliphatic chain into the S1' pocket and exposure of the guanidinomethyl moiety to the solvent.

About this Structure

2D1N 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 the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453., Kohno T, Hochigai H, Yamashita E, Tsukihara T, Kanaoka M, Biochem Biophys Res Commun. 2006 May 26;344(1):315-22. Epub 2006 Mar 27. PMID:16603129

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