5awt

Crystal structure of the SGIP1 mu homology domain in complex with an Eps15 fragment containing two DPF motifs (YDPFGGDPFKG)

spinqualitylabelsall models 5awt, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5awt is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.702Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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