1eh2

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==About this Structure==
==About this Structure==
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1EH2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: NPF. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EH2 OCA]].
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1EH2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: NPF. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EH2 OCA].
==Reference==
==Reference==
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[[Category: signaling domain]]
[[Category: signaling domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:10:40 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:19:12 2007''

Revision as of 13:13, 5 November 2007


1eh2

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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. Structure known Active Site: NPF. 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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