5nin: Difference between revisions
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==Crystal Structure of AKAP79 calmodulin binding domain peptide in complex with Ca2+/Calmodulin== | |||
<StructureSection load='5nin' size='340' side='right' caption='[[5nin]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nin]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NIN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5nin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nin OCA], [http://pdbe.org/5nin PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nin RCSB], [http://www.ebi.ac.uk/pdbsum/5nin PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nin ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/AKAP5_HUMAN AKAP5_HUMAN]] May anchor the PKA protein to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with to the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
AKAP79/150 is essential for coordinating second messenger-responsive enzymes in processes including synaptic long-term depression. Ca(2+) directly regulates AKAP79 through its effector calmodulin (CaM), but the molecular basis of this regulation was previously unknown. Here, we report that CaM recognizes a '1-4-7-8' pattern of hydrophobic amino acids starting at Trp79 in AKAP79. Cross-linking coupled to mass spectrometry assisted mapping of the interaction site. Removal of the CaM-binding sequence in AKAP79 prevents formation of a Ca(2+)-sensitive interface between AKAP79 and calcineurin, and increases resting cellular PKA phosphorylation. We determined a crystal structure of CaM bound to a peptide encompassing its binding site in AKAP79. CaM adopts a highly compact conformation in which its open Ca(2+)-activated C-lobe and closed N-lobe cooperate to recognize a mixed alpha/310 helix in AKAP79. The structure guided a bioinformatic screen to identify potential sites in other proteins that may employ similar motifs for interaction with CaM. | |||
Molecular basis of AKAP79 regulation by calmodulin.,Patel N, Stengel F, Aebersold R, Gold MG Nat Commun. 2017 Nov 22;8(1):1681. doi: 10.1038/s41467-017-01715-w. PMID:29162807<ref>PMID:29162807</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5nin" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gold, M G]] | |||
[[Category: Patel, N]] | |||
[[Category: Akap]] | |||
[[Category: Akap150]] | |||
[[Category: Akap5]] | |||
[[Category: Akap79]] | |||
[[Category: Ca2+]] | |||
[[Category: Calcium]] | |||
[[Category: Calmodulin]] | |||
[[Category: Ef hand]] | |||
[[Category: Signaling protein]] | |||
Revision as of 07:10, 6 December 2017
Crystal Structure of AKAP79 calmodulin binding domain peptide in complex with Ca2+/Calmodulin
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