2d1n: Difference between revisions

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[[Image:2d1n.gif|left|200px]]<br />

[[Image:2d1n.gif|left|200px]]<br /><applet load="2d1n" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2d1n" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2d1n, resolution 2.37Å" />

'''Collagenase-3 (MMP-13) complexed to a hydroxamic acid inhibitor'''<br />

==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.

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 [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].

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==

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[[Category: hydorolase metalloprotease]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12~~ 21:25:27 ~~2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:27 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2d1n.gif|left|200px]]<br />
+[[Image:2d1n.gif|left|200px]]<br /><applet load="2d1n" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2d1n" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2d1n, resolution 2.37&Aring;" />
 '''Collagenase-3 (MMP-13) complexed to a hydroxamic acid inhibitor'''<br />
 ==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.
+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==
-D1N 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].
+D1N 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==
@@ Line 24: / Line 23: @@
 [[Category: hydorolase metalloprotease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:25:27 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:27 2008''