1atl

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(New page: 200px<br /><applet load="1atl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1atl, resolution 1.8&Aring;" /> '''STRUCTURAL INTERACTIO...)
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[[Image:1atl.gif|left|200px]]<br /><applet load="1atl" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1atl.gif|left|200px]]<br /><applet load="1atl" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1atl, resolution 1.8&Aring;" />
caption="1atl, resolution 1.8&Aring;" />
'''STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)'''<br />
'''STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)'''<br />
==Overview==
==Overview==
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The structure of the metalloproteinase and hemorrhagic toxin atrolysin C, form d (EC 3.4.24.42), from the venom of the western diamondback, rattlesnake Crotalus atrox, has been determined to atomic resolution by, x-ray crystallographic methods. This study illuminates the nature of, inhibitor binding with natural (&lt; Glu-Asn-Trp, where &lt; Glu is pyroglutamic, acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is, exceptionally deep; the nature of inhibitor and productive substrate, binding is discussed. Insights gained from the study of these complexes, facilitate the design of potential drugs to treat diseases where matrix, metalloproteinases have been implicated, e.g., arthritis and tumor, metastasis.
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The structure of the metalloproteinase and hemorrhagic toxin atrolysin C form d (EC 3.4.24.42), from the venom of the western diamondback rattlesnake Crotalus atrox, has been determined to atomic resolution by x-ray crystallographic methods. This study illuminates the nature of inhibitor binding with natural (&lt; Glu-Asn-Trp, where &lt; Glu is pyroglutamic acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is exceptionally deep; the nature of inhibitor and productive substrate binding is discussed. Insights gained from the study of these complexes facilitate the design of potential drugs to treat diseases where matrix metalloproteinases have been implicated, e.g., arthritis and tumor metastasis.
==About this Structure==
==About this Structure==
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1ATL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox] with ZN, CA and CH3 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Atrolysin_C Atrolysin C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.42 3.4.24.42] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ATL OCA].
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1ATL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CH3:'>CH3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Atrolysin_C Atrolysin C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.42 3.4.24.42] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATL OCA].
==Reference==
==Reference==
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[[Category: Botos, I.]]
[[Category: Botos, I.]]
[[Category: Doll, R.]]
[[Category: Doll, R.]]
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[[Category: Fox, J.W.]]
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[[Category: Fox, J W.]]
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[[Category: Gomis-Rueth, F.X.]]
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[[Category: Gomis-Rueth, F X.]]
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[[Category: Meyer, E.F.]]
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[[Category: Meyer, E F.]]
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[[Category: Njoroge, F.G.]]
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[[Category: Njoroge, F G.]]
[[Category: Zhang, D.]]
[[Category: Zhang, D.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: metalloendopeptidase]]
[[Category: metalloendopeptidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:07:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:07 2008''

Revision as of 09:48, 21 February 2008

Image:1atl.gif

1atl, resolution 1.8Å

Drag the structure with the mouse to rotate

STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)

Overview

The structure of the metalloproteinase and hemorrhagic toxin atrolysin C form d (EC 3.4.24.42), from the venom of the western diamondback rattlesnake Crotalus atrox, has been determined to atomic resolution by x-ray crystallographic methods. This study illuminates the nature of inhibitor binding with natural (< Glu-Asn-Trp, where < Glu is pyroglutamic acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is exceptionally deep; the nature of inhibitor and productive substrate binding is discussed. Insights gained from the study of these complexes facilitate the design of potential drugs to treat diseases where matrix metalloproteinases have been implicated, e.g., arthritis and tumor metastasis.

About this Structure

1ATL is a Single protein structure of sequence from Crotalus atrox with , and as ligands. Active as Atrolysin C, with EC number 3.4.24.42 Full crystallographic information is available from OCA.

Reference

Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)., Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF, Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8447-51. PMID:8078901

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