4e53: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<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 | <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> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e50|4e50]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e50|4e50]]</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=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> | <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> | ||
| Line 23: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Kumar, V]] | [[Category: Kumar, V]] | ||
[[Category: Sivaraman, J]] | [[Category: Sivaraman, J]] | ||
Revision as of 13:58, 3 August 2017
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
|
| ||||||||||||||||