1kkd: Difference between revisions
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[[Image:1kkd.gif|left|200px]] | [[Image:1kkd.gif|left|200px]] | ||
'''Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)''' | {{Structure | ||
|PDB= 1kkd |SIZE=350|CAPTION= <scene name='initialview01'>1kkd</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= SK2 (KCNN2) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |||
}} | |||
'''Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KKD is a [ | 1KKD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKD OCA]. | ||
==Reference== | ==Reference== | ||
A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin., Wissmann R, Bildl W, Neumann H, Rivard AF, Klocker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B, J Biol Chem. 2002 Feb 8;277(6):4558-64. Epub 2001 Nov 26. PMID:[http:// | A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin., Wissmann R, Bildl W, Neumann H, Rivard AF, Klocker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B, J Biol Chem. 2002 Feb 8;277(6):4558-64. Epub 2001 Nov 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11723128 11723128] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:18:41 2008'' | ||
Revision as of 10:18, 20 March 2008
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| Gene: | SK2 (KCNN2) (Rattus norvegicus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)
Overview
Small conductance Ca(2+)-activated potassium (SK) channels underlie the afterhyperpolarization that follows the action potential in many types of central neurons. SK channels are voltage-independent and gated solely by intracellular Ca(2+) in the submicromolar range. This high affinity for Ca(2+) results from Ca(2+)-independent association of the SK alpha-subunit with calmodulin (CaM), a property unique among the large family of potassium channels. Here we report the solution structure of the calmodulin binding domain (CaMBD, residues 396-487 in rat SK2) of SK channels using NMR spectroscopy. The CaMBD exhibits a helical region between residues 423-437, whereas the rest of the molecule lacks stable overall folding. Disruption of the helical domain abolishes constitutive association of CaMBD with Ca(2+)-free CaM, and results in SK channels that are no longer gated by Ca(2+). The results show that the Ca(2+)-independent CaM-CaMBD interaction, which is crucial for channel function, is at least in part determined by a region different in sequence and structure from other CaM-interacting proteins.
About this Structure
1KKD is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin., Wissmann R, Bildl W, Neumann H, Rivard AF, Klocker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B, J Biol Chem. 2002 Feb 8;277(6):4558-64. Epub 2001 Nov 26. PMID:11723128
Page seeded by OCA on Thu Mar 20 12:18:41 2008
