1inz is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Epsin is a protein that binds to the Eps15 homology (EH) domains, and is involved in clathrin-mediated endocytosis. The epsin N-terminal homology (ENTH) domain (about 140 amino acid residues) is well conserved in eukaryotes and is considered to be important for actin cytoskeleton organization in endocytosis. In this study, we have determined the solution structure of the ENTH domain (residues 1-144) of human epsin by multidimensional nuclear magnetic resonance spectroscopy. In the ENTH-domain structure, seven alpha-helices form a superhelical fold, consisting of two antiparallel two-helix HEAT motifs and one three-helix ARM motif, with a continuous hydrophobic core in the center. We conclude that the seven-helix superhelical fold defines the ENTH domain, and that the previously-reported eight-helix fold of a longer fragment of rat epsin 1 is divided into the authentic ENTH domain and a C-terminal flanking alpha-helix.
Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin.,Koshiba S, Kigawa T, Kikuchi A, Yokoyama S J Struct Funct Genomics. 2002;2(1):1-8. PMID:12836669[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Koshiba S, Kigawa T, Kikuchi A, Yokoyama S. Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin. J Struct Funct Genomics. 2002;2(1):1-8. PMID:12836669
