Journal of Biomolecular NMR

, Volume 39, Issue 4, pp 323–329 | Cite as

EH domain of EHD1

  • Fabien Kieken
  • Marko Jović
  • Naava Naslavsky
  • Steve Caplan
  • Paul L. Sorgen
NMR Structure Note


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.


EHD1 EH domain 



This work was supported by grants from the National Institutes of Health (GM072631, P.L.S.; GM074876, S.C.), the UNMC Eppley Cancer Center Collaborative Research Award (P.L.S. and S.C.), and the Nebraska Center for Cell Signaling fellowship supported by the National Institutes of Health (P20 RR018759, M.J.).


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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular Biology and Eppley Cancer CenterUniversity of Nebraska Medical CenterOmahaUSA

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