5aws
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the SGIP1 mu homology domain in the P1 space group== | |
| + | <StructureSection load='5aws' size='340' side='right' caption='[[5aws]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5aws]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AWS FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5awr|5awr]], [[5awt|5awt]], [[5awu|5awu]]</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=5aws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aws OCA], [http://pdbe.org/5aws PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aws RCSB], [http://www.ebi.ac.uk/pdbsum/5aws PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aws ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SGIP1_HUMAN SGIP1_HUMAN]] May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | FCHo1, FCHo2, and SGIP1 are key regulators of clathrin-mediated endocytosis. Their mu homology domains (muHDs) interact with the C-terminal region of an endocytic scaffold protein, Eps15, containing fifteen Asp-Pro-Phe (DPF) motifs. Here, we show that the high-affinity muHD-binding site in Eps15 is a region encompassing six consecutive DPF motifs, while the minimal muHD-binding unit is two consecutive DPF motifs. We present the crystal structures of the SGIP1 muHD in complex with peptides containing two DPF motifs. The peptides bind to a novel ligand-binding site of the muHD, which is distinct from those of other distantly related muHD-containing proteins. The two DPF motifs, which adopt three-dimensional structures stabilized by sequence-specific intramotif and intermotif interactions, are extensively recognized by the muHD and are both required for binding. Thus, consecutive and singly scattered DPF motifs play distinct roles in muHD binding. | ||
| - | + | Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 mu homology domain.,Shimada A, Yamaguchi A, Kohda D Sci Rep. 2016 Jan 29;6:19565. doi: 10.1038/srep19565. PMID:26822536<ref>PMID:26822536</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5aws" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kohda, D]] | ||
| + | [[Category: Shimada, A]] | ||
| + | [[Category: Yamaguchi, A]] | ||
| + | [[Category: Endocytosis]] | ||
| + | [[Category: Protein-protein interaction]] | ||
Revision as of 02:22, 13 July 2016
Crystal structure of the SGIP1 mu homology domain in the P1 space group
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