6cpi
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of SH3 domain from Shank1== | |
| + | <StructureSection load='6cpi' size='340' side='right' caption='[[6cpi]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6cpi]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CPI 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=6cpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpi OCA], [http://pdbe.org/6cpi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpi RCSB], [http://www.ebi.ac.uk/pdbsum/6cpi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SHAN1_HUMAN SHAN1_HUMAN]] 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 via complexes with GKAP/PSD-95 and Homer, respectively, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction. | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6cpi" 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]] | ||
Revision as of 16:13, 15 August 2018
Solution structure of SH3 domain from Shank1
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