Journal of Structural and Functional Genomics
Online ISSN : 1345-711X
ISSN-L : 1345-711X
Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin
Seizo KoshibaTakanori KigawaAkira KikuchiShigeyuki Yokoyama
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2001 Volume 2-pre Issue 1 Pages L1-L27

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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 α-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 α-helix.

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© 2001 Kluwer Academic Publishers
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