4e53: Difference between revisions

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'''Unreleased structure'''
==Calmodulin and Nm peptide complex==
<StructureSection load='4e53' size='340' side='right' caption='[[4e53]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4e53]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e50|4e50]]</td></tr>
<tr><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://www.rcsb.org/pdb/explore.do?structureId=4e53 RCSB], [http://www.ebi.ac.uk/pdbsum/4e53 PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


The entry 4e53 is ON HOLD  until Paper Publication
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>


Authors: Kumar, V., Sivaraman, J.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


Description: Calmodulin and Nm peptide complex
==See Also==
*[[Calmodulin|Calmodulin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lk3 transgenic mice]]
[[Category: Kumar, V.]]
[[Category: Sivaraman, J.]]
[[Category: Intrinsically unstructured protein]]
[[Category: Iq motif]]
[[Category: Neuromodulin]]
[[Category: Protein binding]]

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