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1eh2
From Proteopedia
| 1eh2, 20 NMR models () | |||||||||
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| Gene: | EPS15 (Homo sapiens) | ||||||||
| Domains: | EH, EH | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES
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.
Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain., de Beer T, Carter RE, Lobel-Rice KE, Sorkin A, Overduin M, Science. 1998 Aug 28;281(5381):1357-60. PMID:9721102
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1EH2 is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- 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. 1998 Aug 28;281(5381):1357-60. PMID:9721102
Page seeded by OCA on Mon Feb 16 14:16:12 2009
