5aws
Crystal structure of the SGIP1 mu homology domain in the P1 space groupCrystal structure of the SGIP1 mu homology domain in the P1 space group
Structural highlights
FunctionSGIP1_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 PubMedFCHo1, 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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