1rww: Difference between revisions

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[[Image:1rww.gif|left|200px]]
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{{STRUCTURE_1rww|  PDB=1rww  |  SCENE=  }}  
{{STRUCTURE_1rww|  PDB=1rww  |  SCENE=  }}  


'''Crystal structure of human caspase-1 in complex with 4-oxo-3-[(6-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-pyridine-3-carbonyl)-amino]-butyric acid'''
===Crystal structure of human caspase-1 in complex with 4-oxo-3-[(6-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-pyridine-3-carbonyl)-amino]-butyric acid===




==Overview==
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Disulfide Tethering was applied to the active site of human caspase-1, resulting in the discovery of a novel, tricyclic molecular fragment that selectively binds in S4. This fragment was developed into a class of potent inhibitors of human caspase-1. Several key analogues determined the optimal distance of the tricycle from the catalytic residues, the relative importance of various features of the tricycle, and the importance of the linker.
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{{ABSTRACT_PUBMED_16274992}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Protein-small molecule inhibitor complex]]
[[Category: Protein-small molecule inhibitor complex]]
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Revision as of 17:25, 27 July 2008

File:1rww.png

Template:STRUCTURE 1rww

Crystal structure of human caspase-1 in complex with 4-oxo-3-[(6-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-pyridine-3-carbonyl)-amino]-butyric acidCrystal structure of human caspase-1 in complex with 4-oxo-3-[(6-{[4-(quinoxalin-2-ylamino)-benzoylamino]-methyl}-pyridine-3-carbonyl)-amino]-butyric acid

Template:ABSTRACT PUBMED 16274992

About this StructureAbout this Structure

1RWW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Tethering identifies fragment that yields potent inhibitors of human caspase-1., Fahr BT, O'Brien T, Pham P, Waal ND, Baskaran S, Raimundo BC, Lam JW, Sopko MM, Purkey HE, Romanowski MJ, Bioorg Med Chem Lett. 2006 Feb;16(3):559-62. Epub 2005 Nov 4. PMID:16274992

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