1eh2
From Proteopedia
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|PDB= 1eh2 |SIZE=350|CAPTION= <scene name='initialview01'>1eh2</scene> | |PDB= 1eh2 |SIZE=350|CAPTION= <scene name='initialview01'>1eh2</scene> | ||
|SITE= <scene name='pdbsite=NPF:TRP+54+Is+Positioned+Within+A+Binding+Site+For+ASN-PRO-P+...'>NPF</scene> | |SITE= <scene name='pdbsite=NPF:TRP+54+Is+Positioned+Within+A+Binding+Site+For+ASN-PRO-P+...'>NPF</scene> | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= EPS15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= EPS15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eh2 OCA], [http://www.ebi.ac.uk/pdbsum/1eh2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eh2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Overduin, M.]] | [[Category: Overduin, M.]] | ||
[[Category: Sorkin, A.]] | [[Category: Sorkin, A.]] | ||
- | [[Category: CA]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
[[Category: ef-hand]] | [[Category: ef-hand]] | ||
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[[Category: signaling domain]] | [[Category: signaling domain]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:02:24 2008'' |
Revision as of 17:02, 30 March 2008
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Sites: | |||||||
Ligands: | |||||||
Gene: | EPS15 (Homo sapiens) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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