This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bma
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1bma" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bma, resolution 1.8Å" /> '''BENZYL METHYL AMINIMI...)
Next diff →
Revision as of 09:38, 20 November 2007
|
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 with CA, SO4 and TFA as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 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 Tue Nov 20 11:45:22 2007
