1kkd
From Proteopedia
(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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| - | [[Image:1kkd.gif|left|200px]]<br /><applet load="1kkd" size=" | + | [[Image:1kkd.gif|left|200px]]<br /><applet load="1kkd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kkd" /> | caption="1kkd" /> | ||
'''Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)'''<br /> | '''Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Small conductance Ca(2+)-activated potassium (SK) channels underlie the | + | 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== | ==About this Structure== | ||
| - | 1KKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1KKD is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Adelman, J | + | [[Category: Adelman, J P.]] |
[[Category: Bentrop, D.]] | [[Category: Bentrop, D.]] | ||
[[Category: Bildl, W.]] | [[Category: Bildl, W.]] | ||
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[[Category: Kloecker, N.]] | [[Category: Kloecker, N.]] | ||
[[Category: Neumann, H.]] | [[Category: Neumann, H.]] | ||
| - | [[Category: Rivard, A | + | [[Category: Rivard, A F.]] |
[[Category: Schulte, U.]] | [[Category: Schulte, U.]] | ||
[[Category: Weitz, D.]] | [[Category: Weitz, D.]] | ||
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[[Category: small-conductance calcium-activated potassium channel]] | [[Category: small-conductance calcium-activated potassium channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:06 2008'' |
Revision as of 11:35, 21 February 2008
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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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