1htd

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[[Image:1htd.gif|left|200px]]<br /><applet load="1htd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1htd.gif|left|200px]]
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caption="1htd, resolution 2.1&Aring;" />
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'''STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-D)'''<br />
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{{Structure
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|PDB= 1htd |SIZE=350|CAPTION= <scene name='initialview01'>1htd</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-D)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1HTD 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> and <scene name='pdbligand=CA:'>CA</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=1HTD OCA].
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1HTD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTD OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8078901 8078901]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8078901 8078901]
[[Category: Atrolysin C]]
[[Category: Atrolysin C]]
[[Category: Crotalus atrox]]
[[Category: Crotalus atrox]]
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[[Category: metalloprotease]]
[[Category: metalloprotease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:41:18 2008''

Revision as of 09:41, 20 March 2008


PDB ID 1htd

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands: and
Activity: Atrolysin C, with EC number 3.4.24.42
Coordinates: save as pdb, mmCIF, xml



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

1HTD is a Single protein structure of sequence from Crotalus atrox. 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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