1e0f

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[[Category: coagulation/crystal structure/heparin-binding site/ hirudin/thrombin inhibitor]]
[[Category: coagulation/crystal structure/heparin-binding site/ hirudin/thrombin inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:41:40 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:03:39 2007''

Revision as of 12:58, 30 October 2007


1e0f, resolution 3.1Å

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CRYSTAL STRUCTURE OF THE HUMAN ALPHA-THROMBIN-HAEMADIN COMPLEX: AN EXOSITE II-BINDING INHIBITOR

Overview

The serine proteinase alpha-thrombin plays a pivotal role in the, regulation of blood fluidity, and therefore constitutes a primary target, in the treatment of various haemostatic disorders. Haemadin is a slow, tight- binding thrombin inhibitor from the land-living leech Haemadipsa, sylvestris. Here we present the 3.1 A crystal structure of the human, alpha-thrombin- haemadin complex. The N-terminal segment of haemadin binds, to the active site of thrombin, forming a parallel beta-strand with, residues Ser214-Gly216 of the proteinase. This mode of binding is similar, to that observed in another leech-derived inhibitor, hirudin. In contrast, to hirudin, however, the markedly acidic C-terminal peptide of haemadin, does not bind the fibrinogen-recognition exosite, but interacts with the, ... [(full description)]

About this Structure

1E0F is a [Protein complex] structure of sequences from [Haemadipsa sylvestris] and [Homo sapiens]. Active as [Thrombin], with EC number [3.4.21.5]. Structure known Active Site: ATE. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor., Richardson JL, Kroger B, Hoeffken W, Sadler JE, Pereira P, Huber R, Bode W, Fuentes-Prior P, EMBO J. 2000 Nov 1;19(21):5650-60. PMID:11060016

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