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1qx5

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[[Image:1qx5.gif|left|200px]]
[[Image:1qx5.gif|left|200px]]
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{{Structure
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|PDB= 1qx5 |SIZE=350|CAPTION= <scene name='initialview01'>1qx5</scene>, resolution 2.54&Aring;
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The line below this paragraph, containing "STRUCTURE_1qx5", creates the "Structure Box" on the page.
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|GENE= CALM1, CAM1, CALM, CAM, CALM2, CAM2, CAMB, CALM3, CAM3, CAMC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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{{STRUCTURE_1qx5| PDB=1qx5 | SCENE= }}
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|RELATEDENTRY=[[1cfc|1CFC]], [[1cfd|1CFD]], [[1cll|1CLL]], [[1g4y|1G4Y]], [[1qx7|1QX7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx5 OCA], [http://www.ebi.ac.uk/pdbsum/1qx5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qx5 RCSB]</span>
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'''Crystal structure of apoCalmodulin'''
'''Crystal structure of apoCalmodulin'''
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[[Category: Miller, M C.]]
[[Category: Miller, M C.]]
[[Category: Schumacher, M A.]]
[[Category: Schumacher, M A.]]
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[[Category: apocalmodulin]]
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[[Category: Apocalmodulin]]
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[[Category: calcium binding protein]]
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[[Category: Calcium binding protein]]
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[[Category: dimer,ef hand]]
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[[Category: Dimer,ef hand]]
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[[Category: domain swap]]
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[[Category: Domain swap]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:48:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:15 2008''
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Revision as of 03:48, 3 May 2008

Image:1qx5.gif

Template:STRUCTURE 1qx5

Crystal structure of apoCalmodulin


Overview

Small conductance Ca2+-activated K+ channels (SK channels) are composed of the pore-forming alpha subunit and calmodulin (CaM). CaM binds to a region of the alpha subunit called the CaM binding domain (CaMBD), located intracellular and immediately C-terminal to the inner helix gate, in either the presence or absence of Ca2+. SK gating occurs when Ca2+ binds the N lobe of CaM thereby transmitting the signal to the attached inner helix gate to open. Here we present crystal structures of apoCaM and apoCaM/SK2 CaMBD complex. Several apoCaM crystal forms with multiple (12) packing environments reveal the same EF hand domain-swapped dimer providing potentially new insight into CaM regulation. The apoCaM/SK2 CaMBD structure, combined with our Ca2+/CaM/CaMBD structure suggests that Ca2+ binding induces folding and dimerization of the CaMBD, which causes large CaMBD-CaM C lobe conformational changes, including a >90 degrees rotation of the region of the CaMBD directly connected to the gate.

About this Structure

1QX5 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex., Schumacher MA, Crum M, Miller MC, Structure. 2004 May;12(5):849-60. PMID:15130477 Page seeded by OCA on Sat May 3 06:48:26 2008

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