6cpj: Difference between revisions

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-'''Unreleased structure'''
-The entry 6cpj is ON HOLD  until Paper Publication
+==Solution structure of SH3 domain from Shank2==
+<StructureSection load='6cpj' size='340' side='right' caption='[[6cpj]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6cpj]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CPJ FirstGlance]. <br>
+</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=6cpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpj OCA], [http://pdbe.org/6cpj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpj RCSB], [http://www.ebi.ac.uk/pdbsum/6cpj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpj ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SHAN2_RAT SHAN2_RAT]] Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. May play a role in the structural and functional organization of the dendritic spine and synaptic junction.<ref>PMID:10506216</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Shank proteins are abundant scaffold proteins in the postsynaptic density (PSD) region of brain synapses. Mutations in Shank proteins are associated with autism, schizophrenia, and Alzheimer's disease. To gain insights into Shank protein interactions at the PSD, we determined the solution structures of the src homology 3 (SH3) domains of all three mammalian Shank proteins. Our findings indicate that they have identical and typical SH3 folding motifs, but unusual target-binding pockets. An investigation into the interaction between the Shank SH3 domains and the proline-rich region of the Cav1.3 calcium channel revealed an atypical interaction in which the highly acidic specificity binding pocket of the SH3 domains binds to a Cav1.3 region containing a cluster of three Arg residues. Our study provides insights into Shank SH3-mediated interactions.
-Authors:
+Solution structures of the SH3 domains from Shank scaffold proteins and their interactions with Cav1.3 calcium channels.,Ishida H, Skorobogatov A, Yamniuk AP, Vogel HJ FEBS Lett. 2018 Jul 29. doi: 10.1002/1873-3468.13209. PMID:30058071<ref>PMID:30058071</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6cpj" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Ishida, H]]
+[[Category: Vogel, H J]]
+[[Category: Postsynaptic density]]
+[[Category: Protein binding]]
+[[Category: Psd]]
+[[Category: Scaffold protein]]