Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin

Seizo Koshiba, Takanori Kigawa, Akira Kikuchi, Shigeyuki Yokoyama

Research output: Contribution to journalArticle

11 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalJournal of Structural and Functional Genomics
Volume2
Issue number1
DOIs
Publication statusPublished - 2002 Jul 8
Externally publishedYes

Keywords

  • ENTH domain
  • Endocytosis
  • Epsin
  • Nuclear magnetic resonance (NMR)
  • Solution structure

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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