1eh2: Difference between revisions

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[[Image:1eh2.gif|left|200px]]
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{{STRUCTURE_1eh2|  PDB=1eh2  |  SCENE=  }}  
{{STRUCTURE_1eh2|  PDB=1eh2  |  SCENE=  }}  


'''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===




==Overview==
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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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{{ABSTRACT_PUBMED_9721102}}


==About this Structure==
==About this Structure==
1EH2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EH2 OCA].  
1EH2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EH2 OCA].  


==Reference==
==Reference==
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[[Category: Npf binding]]
[[Category: Npf binding]]
[[Category: Signaling domain]]
[[Category: Signaling domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:41:15 2008''

Revision as of 21:41, 30 June 2008

File:1eh2.png

Template:STRUCTURE 1eh2

STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9721102

About this Structure

1EH2 is a Single protein structure of sequence from Homo sapiens. Full experimental 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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