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

Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Protein Science Wiley

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

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References (37)

Publisher
Wiley
Copyright
Copyright © 2009 The Protein Society
ISSN
0961-8368
eISSN
1469-896X
DOI
10.1002/pro.258
pmid
19798736
Publisher site
See Article on Publisher Site

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.

Journal

Protein ScienceWiley

Published: Dec 1, 2009

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