1hak
From Proteopedia
(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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| - | [[Image:1hak.gif|left|200px]]<br /> | + | [[Image:1hak.gif|left|200px]]<br /><applet load="1hak" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1hak, resolution 3.0Å" /> | caption="1hak, resolution 3.0Å" /> | ||
'''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLACENTAL ANNEXIN V COMPLEXED WITH K-201 AS A CALCIUM CHANNEL ACTIVITY INHIBITOR'''<br /> | '''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLACENTAL ANNEXIN V COMPLEXED WITH K-201 AS A CALCIUM CHANNEL ACTIVITY INHIBITOR'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HAK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with K21 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1HAK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=K21:'>K21</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: placenta anticoagulant protein-i]] | [[Category: placenta anticoagulant protein-i]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:55:38 2008'' |
Revision as of 13:55, 15 February 2008
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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 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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