1fpc
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(New page: 200px<br /> <applet load="1fpc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpc, resolution 2.3Å" /> '''ACTIVE SITE MIMETIC ...)
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Revision as of 14:49, 12 November 2007
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ACTIVE SITE MIMETIC INHIBITION OF THROMBIN
Contents |
Overview
The structures of two mimetic inhibitor complexes of human alpha-thrombin, have been determined by X-ray crystallography. One mimics a beta-turn with, a bicyclic ring system; the other mimics two different active-site binding, modes. The beta-turn mimetic is used to approximate a turn found in the, conformation of fibrinopeptide A, which is catalytically released by, thrombin in the activation of fibrinogen to fibrin. The binding of the, second mimetic is a hybrid between normal substrate and the abnormal, binding of the potent natural leech inhibitor hirudin. The binding of the, beta-turn mimetic is tenuous, because it is like a substrate, while that, of the substrate-hirudin hybrid is that of a tenacious inhibitor (which it, is). Structurally retrospect modifications for rational design and, improvement of both mimetic inhibitors are proposed.
Disease
Known diseases associated with this structure: Dysprothrombinemia OMIM:[176930], Hyperprothrombinemia OMIM:[176930], Hypoprothrombinemia OMIM:[176930]
About this Structure
1FPC is a Single protein structure of sequence from Homo sapiens with SO3 and ANS as ligands. Active as Thrombin, with EC number 3.4.21.5 Full crystallographic information is available from OCA.
Reference
Active-site mimetic inhibition of thrombin., Mathews II, Tulinsky A, Acta Crystallogr D Biol Crystallogr. 1995 Jul 1;51(Pt 4):550-9. PMID:15299843
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