2kxw

From Proteopedia

(Difference between revisions)

Revision as of 10:50, 11 September 2015

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

Structural highlights

2kxw is a 2 chain structure with sequence from Parte. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	CAM, GSPATT00015825001 (PARTE)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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. [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.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Feldkamp MD, Yu L, Shea MA. Structural and Energetic Determinants of Apo Calmodulin Binding to the IQ Motif of the Na(V)1.2 Voltage-Dependent Sodium Channel. Structure. 2011 Mar 23. PMID:21439835 doi:10.1016/j.str.2011.02.009

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kxw"

@@ Line 2: / Line 2: @@
 <StructureSection load='2kxw' size='340' side='right' caption='[[2kxw]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
 == 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 [http://en.wikipedia.org/wiki/Parte Parte]. 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>
-</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='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 PARTE])</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'>[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://pdbe.org/2kxw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kxw RCSB], [http://www.ebi.ac.uk/pdbsum/2kxw PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2kxw" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Paramecium tetraurelia]]
+[[Category: Parte]]
 [[Category: Feldkamp, M D]]
 [[Category: Shea, M A]]

2kxw

From Proteopedia

Revision as of 10:50, 11 September 2015

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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