2kff | pdb_00002kff

Structure of the C-terminal domain of EHD1 with FNYESTNPFTAK

spinqualitylabelsall models 2kff, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kff is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Related: 2kfh, 2kfg Gene: EHD1, PAST, PAST1, CDABP0131 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [EHD1_HUMAN] Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Eps15 homology (EH)-domain containing proteins are regulators of endocytic membrane trafficking. EH-domain binding to proteins containing the tripeptide NPF has been well characterized, but recent studies have shown that EH-domains are also able to interact with ligands containing DPF or GPF motifs. We demonstrate that the three motifs interact in a similar way with the EH-domain of EHD1, with the NPF motif having the highest affinity due to the presence of an intermolecular hydrogen bond. The weaker affinity for the DPF and GPF motifs suggests that if complex formation occurs in vivo, they may require high ligand concentrations, the presence of successive motifs and/or specific flanking residues. Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.,Kieken F, Jovic M, Tonelli M, Naslavsky N, Caplan S, Sorgen PL Protein Sci. 2009 Dec;18(12):2471-9. PMID:19798736 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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