1ath
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(New page: 200px<br /> <applet load="1ath" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ath, resolution 3.2Å" /> '''THE INTACT AND CLEAV...)
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Revision as of 13:55, 12 November 2007
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THE INTACT AND CLEAVED HUMAN ANTITHROMBIN III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS
Overview
Antithrombin is a member of the serine proteinase inhibitor (serpin), family which contain a flexible reactive site loop that interacts with, and is cleaved by the target proteinase. In cleaved and latent serpins, the reactive site loop is inserted into a large central beta-sheet in the, same molecule, whereas in ovalbumin, a nonfunctional serpin, the reactive, site loop is completely exposed and in an alpha-helical conformation., However, in neither conformation can the reactive site loop bind to target, proteinases. Here we report the structure of an intact and cleaved human, antithrombin complex. The intact reactive site loop is in a novel, conformation that seems well suited for interaction with proteinases such, as thrombin and blood coagulation factor Xa.
About this Structure
1ATH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions., Schreuder HA, de Boer B, Dijkema R, Mulders J, Theunissen HJ, Grootenhuis PD, Hol WG, Nat Struct Biol. 1994 Jan;1(1):48-54. PMID:7656006
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