1avg

From Proteopedia

Revision as of 12:47, 30 October 2007

THROMBIN INHIBITOR FROM TRIATOMA PALLIDIPENNIS

Overview

Triabin, a 142-residue protein from the saliva of the blood-sucking, triatomine bug Triatoma pallidipennis, is a potent and selective thrombin, inhibitor. Its stoichiometric complex with bovine alpha-thrombin was, crystallized, and its crystal structure was solved by Patterson search, methods and refined at 2.6-A resolution to an R value of 0.184. The, analysis revealed that triabin is a compact one-domain molecule, essentially consisting of an eight-stranded beta-barrel. The eight strands, A to H are arranged in the order A-C-B-D-E-F-G-H, with the first four, strands exhibiting a hitherto unobserved up-up-down-down topology. Except, for the B-C inversion, the triabin fold exhibits the regular up-and-down, topology of lipocalins. In contrast to the typical ligand-binding, lipocalins, ... [(full description)]

About this Structure

1AVG is a [Protein complex] structure of sequences from [Bos taurus] and [Triatoma pallidipennis]. Active as [Thrombin], with EC number [3.4.21.5]. Structure known Active Site: ATE. Full crystallographic information is available from [OCA].

Reference

Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug., Fuentes-Prior P, Noeske-Jungblut C, Donner P, Schleuning WD, Huber R, Bode W, Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11845-50. PMID:9342325

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