Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin |
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| Authors: | Koshiba Seizo Kigawa Takanori Kikuchi Akira Yokoyama Shigeyuki |
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| Institution: | (1) Genomic Sciences Center, RIKEN Yokohama Institute, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan;(2) Cellular Signaling Laboratory, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo, 679-5148, Japan;(3) Department of Biochemistry, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima, 734-8551, Japan;(4) Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan |
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| Abstract: | 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  -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 -helix. |
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| Keywords: | epsin ENTH domain endocytosis nuclear magnetic resonance (NMR) solution structure |
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