4e53

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==Calmodulin and Nm peptide complex==
==Calmodulin and Nm peptide complex==
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<StructureSection load='4e53' size='340' side='right' caption='[[4e53]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
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<StructureSection load='4e53' size='340' side='right'caption='[[4e53]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4e53]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E53 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4e53]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E53 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e50|4e50]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69&#8491;</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=4e53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e53 OCA], [http://pdbe.org/4e53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e53 RCSB], [http://www.ebi.ac.uk/pdbsum/4e53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e53 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4e53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e53 OCA], [https://pdbe.org/4e53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e53 RCSB], [https://www.ebi.ac.uk/pdbsum/4e53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e53 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity).[UniProtKB:P0DP23][https://www.uniprot.org/uniprot/NEUM_MOUSE NEUM_MOUSE] This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction.[UniProtKB:P17677]
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Neuromodulin (Nm) and neurogranin (Ng) are neuron-specific substrates of protein kinase C (PKC). Their interactions with Calmodulin (CaM) are crucial for learning and memory formation in neurons. Here, we report the structure of IQ peptides (24aa) of Nm/Ng complexed with CaM and their functional studies with full-length proteins. Nm/Ng and their respective IQ peptides are intrinsically unstructured; however, upon binding with CaM, IQ motifs adopt a helical conformation. Ser41 (Ser36) of Nm (Ng) is located in a negatively charged pocket in the apo CaM and, when phosphorylated, it will repel Nm/Ng from CaM. These observations explain the mechanism by which PKC-induced Ser phosphorylation blocks the association of Nm/Ng with CaM and interrupts several learning- and memory-associated functions. Moreover, the present study identified Arg as a key CaM interacting residue from Nm/Ng. This residue is crucial for CaM-mediated function, as evidenced by the inability of the Ng mutant (Arg-to-Ala) to potentiate synaptic transmission in CA1 hippocampal neurons.
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Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with calmodulin.,Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J Sci Rep. 2013 Mar 6;3:1392. doi: 10.1038/srep01392. PMID:23462742<ref>PMID:23462742</ref>
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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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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<div class="pdbe-citations 4e53" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Kumar, V]]
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[[Category: Large Structures]]
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[[Category: Sivaraman, J]]
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[[Category: Mus musculus]]
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[[Category: Intrinsically unstructured protein]]
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[[Category: Kumar V]]
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[[Category: Iq motif]]
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[[Category: Sivaraman J]]
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[[Category: Neuromodulin]]
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[[Category: Protein binding]]
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Calmodulin and Nm peptide complex

PDB ID 4e53

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