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| ==Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2== | | ==Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2== |
| <StructureSection load='2kxw' size='340' side='right' caption='[[2kxw]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | | <StructureSection load='2kxw' size='340' side='right'caption='[[2kxw]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <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> | | <table><tr><td colspan='2'>[[2kxw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2KXW FirstGlance]. <br> |
| </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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| <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> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxw OCA], [https://pdbe.org/2kxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxw RCSB], [https://www.ebi.ac.uk/pdbsum/2kxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxw ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[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. | | [https://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. |
| <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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| 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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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[Calmodulin|Calmodulin]] | | *[[Calmodulin 3D structures|Calmodulin 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Paramecium tetraurelia]] | | [[Category: Paramecium tetraurelia]] |
| [[Category: Feldkamp, M D]] | | [[Category: Rattus norvegicus]] |
| [[Category: Shea, M A]] | | [[Category: Feldkamp MD]] |
| [[Category: Yu, L]] | | [[Category: Shea MA]] |
| [[Category: Action potential]] | | [[Category: Yu L]] |
| [[Category: Amino acid motif]]
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| [[Category: Animal]]
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| [[Category: Autism]]
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| [[Category: Biomolecular]]
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| [[Category: Brain chemistry]]
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| [[Category: Calcium-binding protein-metal transport complex]]
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| [[Category: Calcium-binding protein]]
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| [[Category: Calmodulin]]
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| [[Category: Channel]]
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| [[Category: Glutamine]]
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| [[Category: Human]]
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| [[Category: Ion channel gating]]
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| [[Category: Iq motif]]
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| [[Category: Isoleucine]]
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| [[Category: Metal transport]]
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| [[Category: Model]]
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| [[Category: Molecular]]
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| [[Category: Nav1 2]]
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| [[Category: Neuronal]]
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| [[Category: Peptide]]
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| [[Category: Protein binding]]
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| [[Category: Protein structure]]
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| [[Category: Sodium channel]]
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| [[Category: Tertiary]]
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| [[Category: Tyrosine]]
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| [[Category: Voltage gated]]
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| [[Category: Voltage-dependent]]
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