1eh2
From Proteopedia
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'''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES''' | '''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES''' | ||
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[[Category: Overduin, M.]] | [[Category: Overduin, M.]] | ||
[[Category: Sorkin, A.]] | [[Category: Sorkin, A.]] | ||
| - | [[Category: | + | [[Category: Calcium binding]] |
| - | [[Category: | + | [[Category: Ef-hand]] |
| - | [[Category: | + | [[Category: Eh domain]] |
| - | [[Category: | + | [[Category: Npf binding]] |
| - | [[Category: | + | [[Category: Signaling domain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:05:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:05, 2 May 2008
STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1EH2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 15:05:34 2008
