1hak: Difference between revisions

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[[Image:1hak.gif|left|200px]]
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[[Image:1hak.png|left|200px]]


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{{STRUCTURE_1hak|  PDB=1hak  |  SCENE=  }}  
{{STRUCTURE_1hak|  PDB=1hak  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLACENTAL ANNEXIN V COMPLEXED WITH K-201 AS A CALCIUM CHANNEL ACTIVITY INHIBITOR'''
===CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLACENTAL ANNEXIN V COMPLEXED WITH K-201 AS A CALCIUM CHANNEL ACTIVITY INHIBITOR===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9398511}}


==About this Structure==
==About this Structure==
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[[Category: Lipocortin v]]
[[Category: Lipocortin v]]
[[Category: Placenta anticoagulant protein-i]]
[[Category: Placenta anticoagulant protein-i]]
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Revision as of 04:54, 1 July 2008

File:1hak.png

Template:STRUCTURE 1hak

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLACENTAL ANNEXIN V COMPLEXED WITH K-201 AS A CALCIUM CHANNEL ACTIVITY INHIBITOR

Template:ABSTRACT PUBMED 9398511

About this Structure

1HAK is a Single protein structure of sequence from Homo sapiens. 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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