5awt: Difference between revisions

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-'''Unreleased structure'''
-The entry 5awt is ON HOLD
+==Crystal structure of the SGIP1 mu homology domain in complex with an Eps15 fragment containing two DPF motifs (YDPFGGDPFKG)==
+<StructureSection load='5awt' size='340' side='right'caption='[[5awt]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5awt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWT 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]] 2.702&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5awt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awt OCA], [https://pdbe.org/5awt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awt RCSB], [https://www.ebi.ac.uk/pdbsum/5awt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awt ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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.
-Authors: Shimada, A., Yamaguchi, A., Kohda, D.
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Shimada, A]]
+<div class="pdbe-citations 5awt" style="background-color:#fffaf0;"></div>
-[[Category: Yamaguchi, A]]
+== References ==
-[[Category: Kohda, D]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Kohda D]]
+[[Category: Shimada A]]
+[[Category: Yamaguchi A]]