2kxw

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[[Image:2kxw.png|left|200px]]
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==Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2==
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<StructureSection load='2kxw' size='340' side='right' caption='[[2kxw]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2kxw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KXW FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAM, GSPATT00015825001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5888 Paramecium tetraurelia])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kxw RCSB], [http://www.ebi.ac.uk/pdbsum/2kxw PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CALM_PARTE CALM_PARTE]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. [[http://www.uniprot.org/uniprot/SCN2A_RAT SCN2A_RAT]] Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The neuronal voltage-dependent sodium channel (Na(v)1.2), essential for generation and propagation of action potentials, is regulated by calmodulin (CaM) binding to the IQ motif in its alpha subunit. A peptide (Na(v)1.2(IQp), KRKQEEVSAIVIQRAYRRYLLKQKVKK) representing the IQ motif had higher affinity for apo CaM than (Ca(2+))(4)-CaM. Association was mediated solely by the C-domain of CaM. A solution structure (2KXW.pdb) of apo (13)C,(15)N-CaM C-domain bound to Na(v)1.2(IQp) was determined with NMR. The region of Na(v)1.2(IQp) bound to CaM was helical; R1902, an Na(v)1.2 residue implicated in familial autism, did not contact CaM. The apo C-domain of CaM in this complex shares features of the same domain bound to myosin V IQ motifs (2IX7) and bound to an SK channel peptide (1G4Y) that does not contain an IQ motif. Thermodynamic and structural studies of CaM-Na(v)1.2(IQp) interactions show that apo and (Ca(2+))(4)-CaM adopt distinct conformations that both permit tight association with Na(v)1.2(IQp) during gating.
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{{STRUCTURE_2kxw| PDB=2kxw | SCENE= }}
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Structural and Energetic Determinants of Apo Calmodulin Binding to the IQ Motif of the Na(V)1.2 Voltage-Dependent Sodium Channel.,Feldkamp MD, Yu L, Shea MA Structure. 2011 Mar 23. PMID:21439835<ref>PMID:21439835</ref>
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===Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_21439835}}
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==About this Structure==
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[[2kxw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXW OCA].
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==See Also==
==See Also==
*[[Calmodulin|Calmodulin]]
*[[Calmodulin|Calmodulin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021439835</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Paramecium tetraurelia]]
[[Category: Paramecium tetraurelia]]
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[[Category: Feldkamp, M D.]]
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[[Category: Feldkamp, M D]]
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[[Category: Shea, M A.]]
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[[Category: Shea, M A]]
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[[Category: Yu, L.]]
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[[Category: Yu, L]]
[[Category: Action potential]]
[[Category: Action potential]]
[[Category: Amino acid motif]]
[[Category: Amino acid motif]]

Revision as of 15:27, 25 December 2014

Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2

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