2m0k

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(Difference between revisions)

Revision as of 04:44, 10 September 2015

3D Structure of Calmodulin and Calmodulin Binding Domain of Rat Olfactory Cyclic Nucleotide-Gated Ion Channel

Structural highlights

2m0k is a 2 chain structure with sequence from Buffalo rat and Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2m0j
Gene:	CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2, CAM3, CAMC, CAMIII (HUMAN), Cnga2, Cncg2 (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CNGA2_RAT] Odorant signal transduction is probably mediated by a G-protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons.

Publication Abstract from PubMed

Calmodulin (CaM), the primary intracellular Ca(2+) receptor, regulates a large number of key enzymes and controls a wide spectrum of important biological responses. Recognition between CaM and its target sequence in rat olfactory cyclic nucleotide-gated ion channel (OLFp) was investigated by circular dichroism (CD), fluorescence, and NMR spectroscopy. Fluorescence data showed the OLFp tightly bound to CaM with a dissociation constant of 12 nM in a 1:1 stoichiometry. Far-UV CD data showed that approximately 60% of OLFp residues formed alpha-helical structures when associated with CaM. NMR data showed that most of the (15)N-(1)H HSQC cross-peaks of the (15)N-labeled CaM not only shifted but also split into two sets of peaks upon association with the OLFp. Our data indicated that the two distinct CaM/OLFp complexes existed simultaneously with stable structures that were not interexchangeable within the NMR time scale. In light of the palindromic sequence of OLFp (FQRIVRLVGVIRDW) for CaM targeting, we proposed that the helical OLFp with C2 symmetry may bind to CaM in two orientations. This hypothesis is supported by the observation that only one set of (15)N-(1)H HSQC cross-peaks of the (15)N-labeled CaM was detected upon association with OLFp-M13 chimeric peptide (OLFMp), a mutated OLFp lacking the palindromic feature. The binding specificity of OLFMp to CaM was restored when the palindromic feature was destroyed. Binding modes of CaM/OLFp and CaM/OLFMp simulated by molecular docking were in accord with their distinct patterns observed in HSQC spectra. Our studies suggest that the palindromic residues in OLFp are crucial for the orientation-specific recognition by CaM.

Binding orientation and specificity of calmodulin to rat olfactory cyclic nucleotide-gated ion channel.,Irene D, Huang JW, Chung TY, Li FY, Tzen JT, Lin TH, Chyan CL J Biomol Struct Dyn. 2013 Apr;31(4):414-25. doi: 10.1080/07391102.2012.703069., Epub 2012 Aug 9. PMID:22877078^[1]

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

References

↑ Irene D, Huang JW, Chung TY, Li FY, Tzen JT, Lin TH, Chyan CL. Binding orientation and specificity of calmodulin to rat olfactory cyclic nucleotide-gated ion channel. J Biomol Struct Dyn. 2013 Apr;31(4):414-25. doi: 10.1080/07391102.2012.703069., Epub 2012 Aug 9. PMID:22877078 doi:http://dx.doi.org/10.1080/07391102.2012.703069

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/2m0k"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2m0j|2m0j]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2, CAM3, CAMC, CAMIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Cnga2, Cncg2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=2m0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m0k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m0k RCSB], [http://www.ebi.ac.uk/pdbsum/2m0k 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=2m0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m0k OCA], [http://pdbe.org/2m0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m0k RCSB], [http://www.ebi.ac.uk/pdbsum/2m0k PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2m0k" style="background-color:#fffaf0;"></div>
 ==See Also==

2m0k

From Proteopedia

Revision as of 04:44, 10 September 2015

3D Structure of Calmodulin and Calmodulin Binding Domain of Rat Olfactory Cyclic Nucleotide-Gated Ion Channel

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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