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1btw
From Proteopedia
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EPISELECTION: NOVEL KI ~NANOMOLAR INHIBITORS OF SERINE PROTEASES SELECTED BY BINDING OR CHEMISTRY ON AN ENZYME SURFACE
Overview
A novel class of mechanism-based inhibitors of the serine proteases is, developed using epitaxial selection. Tripeptide boronates esterified by an, alcohol or alcohols at the boron retain the tight binding to trypsin-like, enzymes associated with transition-state analogs and incorporate, additional groups that can be utilized for selectivity between proteases., Formed by reaction of a series of alcohols with the inhibitor boronate, oxygen(s), the most structurally compatible alcohol-derivatized inhibitors, are either selected by binding to the enzyme (epitaxial selection) or, assembled by epitaxial reaction on the enzyme surface. Mass spectrometry, of the derivatized boronates and X-ray crystallography of the complexes, identify the chemical structures and the three-dimensional interactions of, inhibitors generated. This scheme also engineers novel, potent (Ki, approximately 7 nM), and more specific inhibitors of individual serine, proteases, by derivitizations of compounds obtained by epitaxial, selection.
About this Structure
1BTW is a Single protein structure of sequence from Bos taurus with CA and PDO as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface., Katz BA, Finer-Moore J, Mortezaei R, Rich DH, Stroud RM, Biochemistry. 1995 Jul 4;34(26):8264-80. PMID:7599119
Page seeded by OCA on Tue Nov 20 11:55:01 2007
