View source for 5awu


==Crystal structure of the SGIP1 mu homology domain in complex with an Eps15 fragment containing two DPF motifs (YDPFKGSDPFA)==
<StructureSection load='5awu' size='340' side='right'caption='[[5awu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5awu]] 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=5AWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWU 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]] 2.7&#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=5awu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awu OCA], [https://pdbe.org/5awu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awu RCSB], [https://www.ebi.ac.uk/pdbsum/5awu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awu 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.

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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5awu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kohda D]]
[[Category: Shimada A]]
[[Category: Yamaguchi A]]