1g4y
From Proteopedia
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|PDB= 1g4y |SIZE=350|CAPTION= <scene name='initialview01'>1g4y</scene>, resolution 1.60Å | |PDB= 1g4y |SIZE=350|CAPTION= <scene name='initialview01'>1g4y</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= RAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= RAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g4y OCA], [http://www.ebi.ac.uk/pdbsum/1g4y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g4y RCSB]</span> | ||
}} | }} | ||
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[[Category: Rivard, A.]] | [[Category: Rivard, A.]] | ||
[[Category: Schumacher, M A.]] | [[Category: Schumacher, M A.]] | ||
- | [[Category: CA]] | ||
- | [[Category: SO4]] | ||
[[Category: calmodulin]] | [[Category: calmodulin]] | ||
[[Category: calmodulin binding domain (cambd)]] | [[Category: calmodulin binding domain (cambd)]] | ||
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[[Category: small-conductance calcium-activated potassium channel]] | [[Category: small-conductance calcium-activated potassium channel]] | ||
- | ''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 20:36:40 2008'' |
Revision as of 17:36, 30 March 2008
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, resolution 1.60Å | |||||||
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Ligands: | , | ||||||
Gene: | RAT (Rattus norvegicus) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
1.60 A CRYSTAL STRUCTURE OF THE GATING DOMAIN FROM SMALL CONDUCTANCE POTASSIUM CHANNEL COMPLEXED WITH CALCIUM-CALMODULIN
Overview
Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. Here we report the 1.60 A crystal structure of the SK channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe has bound Ca2+, the structure provides a view of both calcium-dependent and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.
About this Structure
1G4Y is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin., Schumacher MA, Rivard AF, Bachinger HP, Adelman JP, Nature. 2001 Apr 26;410(6832):1120-4. PMID:11323678
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