EH domain of EHD1

Fabien Kieken, Marko Jović, Naava Naslavsky, Steve Caplan, Paul L. Sorgen

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

EHD1 is a member of the mammalian C-terminal Eps15 homology domain (EH) containing protein family, and regulates the recycling of various receptors from the endocytic recycling compartment to the plasma membrane. The EH domain of EHD1 binds to proteins containing either an Asn-Pro-Phe or Asp-Pro-Phe motif, and plays an important role in the subcellular localization and function of EHD1. Thus far, the structures of five N-terminal EH domains from other proteins have been solved, but to date, the structure of the EH domains from the four C-terminal EHD family paralogs remains unknown. In this study, we have assigned the 133 C-terminal residues of EHD1, which includes the EH domain, and solved its solution structure. While the overall structure resembles that of the second of the three N-terminal Eps15 EH domains, potentially significant differences in surface charge and the structure of the tripeptide-binding pocket are discussed.

Original languageEnglish (US)
Pages (from-to)323-329
Number of pages7
JournalJournal of Biomolecular NMR
Volume39
Issue number4
DOIs
StatePublished - Dec 1 2007

Keywords

  • EH domain
  • EHD1

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy

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    Kieken, F., Jović, M., Naslavsky, N., Caplan, S., & Sorgen, P. L. (2007). EH domain of EHD1. Journal of Biomolecular NMR, 39(4), 323-329. https://doi.org/10.1007/s10858-007-9196-0