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- Title
Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.
- Authors
de Beer, T; Carter, R E; Lobel-Rice, K E; Sorkin, A; Overduin, M
- 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.
- Publication
Science (New York, N.Y.), 1998, Vol 281, Issue 5381, p1357
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.281.5381.1357