1eh2
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(New page: 200px<br /> <applet load="1eh2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eh2" /> '''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMA...)
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Revision as of 19:39, 29 October 2007
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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] with CA as [ligand]. 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
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