1hak
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(New page: 200px<br /> <applet load="1hak" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hak, resolution 3.0Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 15:08, 12 November 2007
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CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLACENTAL ANNEXIN V COMPLEXED WITH K-201 AS A CALCIUM CHANNEL ACTIVITY INHIBITOR
Overview
The crystal structure of recombinant human annexin V complexed with K-201, an inhibitor of the calcium ion channel activity of annexin V, was solved, at 3.0 A by molecular replacement including the apo and high-calcium, forms. K-201 was bound at the hinge region cavity formed by the N-terminal, strand and domains II, III and IV, at the side opposite the calcium and, membrane-binding surface, in an L-shaped conformation. Based on the, complex and other annexin structures, K-201 is proposed to restrain the, hinge movement of annexin V in an allosteric manner, resulting in the, inhibition of calcium movement across the annexin V molecule.
About this Structure
1HAK is a Single protein structure of sequence from Homo sapiens with K21 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor., Kaneko N, Ago H, Matsuda R, Inagaki E, Miyano M, J Mol Biol. 1997 Nov 21;274(1):16-20. PMID:9398511
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