5zz9
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of Homer2 EVH1/Drebrin PPXXF complex== | |
+ | <StructureSection load='5zz9' size='340' side='right'caption='[[5zz9]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5zz9]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZZ9 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zz9 OCA], [https://pdbe.org/5zz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zz9 RCSB], [https://www.ebi.ac.uk/pdbsum/5zz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zz9 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/HOME2_MOUSE HOME2_MOUSE] Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Drebrin is an actin bundling protein that plays critical roles in synaptic spine development and plasticity. Homer, one of the most abundant scaffolding proteins in postsynaptic density, interacts with Drebrin's C-terminal PPXXF motifs using its Ena/VASP homology 1 (EVH1) domain. However, the molecular mechanism and biological function of this interaction remain unclear. Here we show that Homer specifically binds to the first but not the second PPXXF motif in Drebrin. The crystal structure of Drebrin-Homer binding motif 1 in complex with Homer EVH1 reveals a consensus Homer EVH1 binding motif. Homer tetramer promotes actin bundling activity of Drebrin in vitro and stimulates Drebrin-induced filopodia formation and elongation in cells. We further show that monomeric Homer1a antagonizes Homer1b in promoting Drebrin-stimulated actin bundling. Our study suggests a potential regulatory role of Homer1 in modulating excitatory synaptic spine homeostatic scaling via binding to Drebrin. | ||
- | + | Homer Tetramer Promotes Actin Bundling Activity of Drebrin.,Li Z, Liu H, Li J, Yang Q, Feng Z, Li Y, Yang H, Yu C, Wan J, Liu W, Zhang M Structure. 2018 Nov 5. pii: S0969-2126(18)30372-1. doi:, 10.1016/j.str.2018.10.011. PMID:30503778<ref>PMID:30503778</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 5zz9" style="background-color:#fffaf0;"></div> |
- | [[Category: Li | + | == References == |
- | [[Category: Liu | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Mus musculus]] | ||
+ | [[Category: Li J]] | ||
+ | [[Category: Li Z]] | ||
+ | [[Category: Liu H]] | ||
+ | [[Category: Liu W]] | ||
+ | [[Category: Zhang M]] |
Current revision
Crystal structure of Homer2 EVH1/Drebrin PPXXF complex
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Categories: Homo sapiens | Large Structures | Mus musculus | Li J | Li Z | Liu H | Liu W | Zhang M