4e53: Difference between revisions
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==Calmodulin and Nm peptide complex== | ==Calmodulin and Nm peptide complex== | ||
<StructureSection load='4e53' size='340' side='right' caption='[[4e53]], [[Resolution|resolution]] 2.69Å' scene=''> | <StructureSection load='4e53' size='340' side='right'caption='[[4e53]], [[Resolution|resolution]] 2.69Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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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</div> | </div> | ||
<div class="pdbe-citations 4e53" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4e53" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Calmodulin 3D structures|Calmodulin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Kumar, V]] | [[Category: Kumar, V]] | ||
[[Category: Sivaraman, J]] | [[Category: Sivaraman, J]] |
Revision as of 20:59, 14 August 2019
Calmodulin and Nm peptide complexCalmodulin and Nm peptide complex
Structural highlights
Publication Abstract from PubMedNeuromodulin (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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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