1bma
From Proteopedia
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[[Image:1bma.gif|left|200px]] | [[Image:1bma.gif|left|200px]] | ||
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'''BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE''' | '''BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE''' | ||
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[[Category: Petsko, G A.]] | [[Category: Petsko, G A.]] | ||
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
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Revision as of 08:41, 2 May 2008
BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE
Overview
The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar interactions with the subsites on the elastase surface. Because aminimides are readily synthesized from a wide variety of starting materials, they form the basis for a combinatorial chemistry approach to rational drug design.
About this Structure
1BMA is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Interaction of a peptidomimetic aminimide inhibitor with elastase., Peisach E, Casebier D, Gallion SL, Furth P, Petsko GA, Hogan JC Jr, Ringe D, Science. 1995 Jul 7;269(5220):66-9. PMID:7604279 Page seeded by OCA on Fri May 2 11:41:41 2008