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1d5j

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(New page: 200px<br /> <applet load="1d5j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d5j, resolution 2.6&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1d5j.gif|left|200px]]<br /><applet load="1d5j" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1d5j" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1d5j, resolution 2.6&Aring;" />
caption="1d5j, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A THIAZEPINE BASED INHIBITOR.'''<br />
'''CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A THIAZEPINE BASED INHIBITOR.'''<br />
==Overview==
==Overview==
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The synthesis and enzyme inhibition data for a series of thiazine- and, thiazepine-based matrix metalloproteinase (MMP) inhibitors are described., The thiazine- and thiazepine-based inhibitors were discovered by, optimization of hetererocyclic sulfonamide-based inhibitors. The most, potent series of inhibitors was obtained by modification of the amino acid, D-penicillamine. This amino acid provides a gem-dimethyl group on the, thiazine or thiazepine ring which has a dramatic effect on the in vitro, potency of this series. In particular, the sulfide 4a and the sulfone 5a, were potent, broad-spectrum inhibitors of the MMPs with IC(50)'s against, MMP-1 of 0.8 and 1.9 nM, respectively. The binding mode of this novel, thiazepine-based series of MMP inhibitors was established based on X-ray, crystallography of the complex of stromelysin and 4a.
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The synthesis and enzyme inhibition data for a series of thiazine- and thiazepine-based matrix metalloproteinase (MMP) inhibitors are described. The thiazine- and thiazepine-based inhibitors were discovered by optimization of hetererocyclic sulfonamide-based inhibitors. The most potent series of inhibitors was obtained by modification of the amino acid D-penicillamine. This amino acid provides a gem-dimethyl group on the thiazine or thiazepine ring which has a dramatic effect on the in vitro potency of this series. In particular, the sulfide 4a and the sulfone 5a were potent, broad-spectrum inhibitors of the MMPs with IC(50)'s against MMP-1 of 0.8 and 1.9 nM, respectively. The binding mode of this novel thiazepine-based series of MMP inhibitors was established based on X-ray crystallography of the complex of stromelysin and 4a.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1D5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN, CA and MM3 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Stromelysin_1 Stromelysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D5J OCA].
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1D5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MM3:'>MM3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Stromelysin_1 Stromelysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5J OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Stromelysin 1]]
[[Category: Stromelysin 1]]
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[[Category: Almstead, N.G.]]
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[[Category: Almstead, N G.]]
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[[Category: Bradley, R.S.]]
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[[Category: Bradley, R S.]]
[[Category: De, B.]]
[[Category: De, B.]]
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[[Category: Natchus, M.G.]]
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[[Category: Natchus, M G.]]
[[Category: Pikul, S.]]
[[Category: Pikul, S.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: zinc protease]]
[[Category: zinc protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:29:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:11 2008''

Revision as of 10:13, 21 February 2008


1d5j, resolution 2.6Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A THIAZEPINE BASED INHIBITOR.

Contents

Overview

The synthesis and enzyme inhibition data for a series of thiazine- and thiazepine-based matrix metalloproteinase (MMP) inhibitors are described. The thiazine- and thiazepine-based inhibitors were discovered by optimization of hetererocyclic sulfonamide-based inhibitors. The most potent series of inhibitors was obtained by modification of the amino acid D-penicillamine. This amino acid provides a gem-dimethyl group on the thiazine or thiazepine ring which has a dramatic effect on the in vitro potency of this series. In particular, the sulfide 4a and the sulfone 5a were potent, broad-spectrum inhibitors of the MMPs with IC(50)'s against MMP-1 of 0.8 and 1.9 nM, respectively. The binding mode of this novel thiazepine-based series of MMP inhibitors was established based on X-ray crystallography of the complex of stromelysin and 4a.

Disease

Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250]

About this Structure

1D5J is a Single protein structure of sequence from [1] with , and as ligands. Active as Stromelysin 1, with EC number 3.4.24.17 Full crystallographic information is available from OCA.

Reference

Design, synthesis, and biological evaluation of potent thiazine- and thiazepine-based matrix metalloproteinase inhibitors., Almstead NG, Bradley RS, Pikul S, De B, Natchus MG, Taiwo YO, Gu F, Williams LE, Hynd BA, Janusz MJ, Dunaway CM, Mieling GE, J Med Chem. 1999 Nov 4;42(22):4547-62. PMID:10579818

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