1hak
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hak OCA], [http://www.ebi.ac.uk/pdbsum/1hak PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hak RCSB]</span> | ||
}} | }} | ||
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[[Category: Inagaki, E.]] | [[Category: Inagaki, E.]] | ||
[[Category: Miyano, M.]] | [[Category: Miyano, M.]] | ||
| - | [[Category: K21]] | ||
[[Category: 35kda calelectrin]] | [[Category: 35kda calelectrin]] | ||
[[Category: annexin v]] | [[Category: annexin v]] | ||
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[[Category: placenta anticoagulant protein-i]] | [[Category: placenta anticoagulant protein-i]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:01:09 2008'' |
Revision as of 18:01, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CDNA (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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