Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.
Publication
, Journal Article
de Beer, T; Carter, RE; Lobel-Rice, KE; Sorkin, A; Overduin, M
Published in: Science (New York, N.Y.)
August 1998
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.
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Published In
Science (New York, N.Y.)
DOI
EISSN
1095-9203
ISSN
0036-8075
Publication Date
August 1998
Volume
281
Issue
5381
Start / End Page
1357 / 1360
Related Subject Headings
- Signal Transduction
- Protein Structure, Secondary
- Protein Folding
- Protein Conformation
- Protein Binding
- Phosphoproteins
- Oligopeptides
- Nuclear Magnetic Resonance, Biomolecular
- Mutation
- Molecular Sequence Data
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de Beer, T., Carter, R. E., Lobel-Rice, K. E., Sorkin, A., & Overduin, M. (1998). Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Science (New York, N.Y.), 281(5381), 1357–1360. https://doi.org/10.1126/science.281.5381.1357
Beer, T. de, R. E. Carter, K. E. Lobel-Rice, A. Sorkin, and M. Overduin. “Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.” Science (New York, N.Y.) 281, no. 5381 (August 1998): 1357–60. https://doi.org/10.1126/science.281.5381.1357.
de Beer T, Carter RE, Lobel-Rice KE, Sorkin A, Overduin M. Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Science (New York, NY). 1998 Aug;281(5381):1357–60.
de Beer, T., et al. “Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.” Science (New York, N.Y.), vol. 281, no. 5381, Aug. 1998, pp. 1357–60. Epmc, doi:10.1126/science.281.5381.1357.
de Beer T, Carter RE, Lobel-Rice KE, Sorkin A, Overduin M. Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Science (New York, NY). 1998 Aug;281(5381):1357–1360.
Published In
Science (New York, N.Y.)
DOI
EISSN
1095-9203
ISSN
0036-8075
Publication Date
August 1998
Volume
281
Issue
5381
Start / End Page
1357 / 1360
Related Subject Headings
- Signal Transduction
- Protein Structure, Secondary
- Protein Folding
- Protein Conformation
- Protein Binding
- Phosphoproteins
- Oligopeptides
- Nuclear Magnetic Resonance, Biomolecular
- Mutation
- Molecular Sequence Data