1kkd
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(New page: 200px<br /><applet load="1kkd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kkd" /> '''Solution structure of the calmodulin binding...)
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Revision as of 17:12, 20 November 2007
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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
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