1kkd

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[[Image:1kkd.gif|left|200px]]<br /><applet load="1kkd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kkd.gif|left|200px]]
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caption="1kkd" />
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'''Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)'''<br />
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{{Structure
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|PDB= 1kkd |SIZE=350|CAPTION= <scene name='initialview01'>1kkd</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= SK2 (KCNN2) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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}}
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'''Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11723128 11723128]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:06 2008''
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''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


PDB ID 1kkd

Drag the structure with the mouse to rotate
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

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