1eh2
From Proteopedia
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| - | [[Image:1eh2.gif|left|200px]]<br /> | + | [[Image:1eh2.gif|left|200px]]<br /><applet load="1eh2" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1eh2" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1eh2" /> | caption="1eh2" /> | ||
'''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES'''<br /> | '''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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]. | + | 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]. Known structural/functional Site: <scene name='pdbsite=NPF:TRP 54 Is Positioned Within A Binding Site For ASN-PRO-P ...'>NPF</scene>. 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]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:12:36 2007'' |
Revision as of 13:02, 18 December 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. Known structural/functional Site: . 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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