Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1

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

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Eps15 homology (EH)-domain containing proteins are regulators of endocytic membrane trafficking. EH-domain binding to proteins containing the tripeptide NPF has been well characterized, but recent studies have shown that EH-domains are also able to interact with ligands containing DPF or GPF motifs. We demonstrate that the three motifs interact in a similar way with the EH-domain of EHD1, with the NPF motif having the highest affinity due to the presence of an intermolecular hydrogen bond. The weaker affinity for the DPF and GPF motifs suggests that if complex formation occurs in vivo, they may require high ligand concentrations, the presence of successive motifs and/or specific flanking residues. Published by Wiley-Blackwell.

Original languageEnglish (US)
Pages (from-to)2471-2479
Number of pages9
JournalProtein Science
Volume18
Issue number12
DOIs
StatePublished - Dec 1 2009

Keywords

  • EH-domain
  • EHD1
  • Endocytic transport
  • NPF motif

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1'. Together they form a unique fingerprint.

  • Cite this