SGD Paper 
de Beer T, et al. (1998) Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Science 281(5381):1357-60
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.
| Status: Published | Type: Journal Article | PubMed ID: 9721102 |
Topics addressed in this paper
Number of different genes curated to this paper: 2
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