1t1f: Difference between revisions

Revision as of 04:07, 28 July 2008

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File:1t1f.png

Template:STRUCTURE 1t1f

Crystal Structure of Native Antithrombin in its Monomeric FormCrystal Structure of Native Antithrombin in its Monomeric Form

Template:ABSTRACT PUBMED 16973611

About this StructureAbout this Structure

1T1F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of monomeric native antithrombin reveals a novel reactive center loop conformation., Johnson DJ, Langdown J, Li W, Luis SA, Baglin TP, Huntington JA, J Biol Chem. 2006 Nov 17;281(46):35478-86. Epub 2006 Sep 13. PMID:16973611

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OCA

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 {{STRUCTURE_1t1f|  PDB=1t1f  |  SCENE=  }}
-'''Crystal Structure of Native Antithrombin in its Monomeric Form'''
+===Crystal Structure of Native Antithrombin in its Monomeric Form===
-==Overview==
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-The poor inhibitory activity of circulating antithrombin (AT) is critical to the formation of blood clots at sites of vascular damage. AT becomes an efficient inhibitor of the coagulation proteases only after binding to a specific heparin pentasaccharide, which alters the conformation of the reactive center loop (RCL). The molecular basis of this activation event lies at the heart of the regulation of hemostasis and accounts for the anticoagulant properties of the low molecular weight heparins. Although several structures of AT have been solved, the conformation of the RCL in native AT remains unknown because of the obligate crystal contact between the RCL of native AT and its latent counterpart. Here we report the crystallographic structure of a variant of AT in its monomeric native state. The RCL shifted approximately 20 A, and a salt bridge was observed between the P1 residue (Arg-393) and Glu-237. This contact explains the effect of mutations at the P1 position on the affinity of AT for heparin and also the properties of AT-Truro (E237K). The relevance of the observed conformation was verified through mutagenesis studies and by solving structures of the same variant in different crystal forms. We conclude that the poor inhibitory activity of the circulating form of AT is partially conferred by intramolecular contacts that restrain the RCL, orient the P1 residue away from attacking proteases, and additionally block the exosite utilized in protease recognition.
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+{{ABSTRACT_PUBMED_16973611}}
 ==About this Structure==
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 [[Category: Thrombin]]
 [[Category: X-ray crystallography]]
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