1qx5
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1cfc|1CFC]], [[1cfd|1CFD]], [[1cll|1CLL]], [[1g4y|1G4Y]], [[1qx7|1QX7]] | ||
| + | |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> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: apocalmodulin]] | [[Category: apocalmodulin]] | ||
[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
| - | [[Category: dimer]] | + | [[Category: dimer,ef hand]] |
[[Category: domain swap]] | [[Category: domain swap]] | ||
| - | [[Category: ef hand]] | ||
| - | ''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 23:20:15 2008'' |
Revision as of 20:20, 30 March 2008
| |||||||
| , resolution 2.54Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | CALM1, CAM1, CALM, CAM, CALM2, CAM2, CAMB, CALM3, CAM3, CAMC (Rattus norvegicus) | ||||||
| Related: | 1CFC, 1CFD, 1CLL, 1G4Y, 1QX7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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