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    Science. 1998 Aug 28;281(5381):1357-60.

    Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.

    de Beer T, Carter RE, Lobel-Rice KE, Sorkin A, Overduin M.

    Source

    Department of Pharmacology, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, CO 80262, USA.

    Abstract

    Eps15 homology (EH) domains are eukaryotic signaling modules that recognize proteins containing Asn-Pro-Phe (NPF) sequences. The structure of the central EH domain of Eps15 has been solved by heteronuclear magnetic resonance spectroscopy. The fold consists of a pair of EF hand motifs, the second of which binds tightly to calcium. The NPF peptide is bound in a hydrophobic pocket between two alpha helices, and binding is mediated by a critical aromatic interaction as revealed by structure-based mutagenesis. The fold is predicted to be highly conserved among 30 identified EH domains and provides a structural basis for defining EH-mediated events in protein trafficking and growth factor signaling.

    PMID:
    9721102
    [PubMed - indexed for MEDLINE]
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