1f8h: Difference between revisions

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[[Image:1f8h.gif|left|200px]]
[[Image:1f8h.gif|left|200px]]


{{Structure
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|DOMAIN=
{{STRUCTURE_1f8h| PDB=1f8h  | SCENE= }}  
|RELATEDENTRY=[[1eh2|1eh2]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f8h OCA], [http://www.ebi.ac.uk/pdbsum/1f8h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f8h RCSB]</span>
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'''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 IN COMPLEX WITH PTGSSSTNPFR'''
'''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 IN COMPLEX WITH PTGSSSTNPFR'''
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[[Category: Overduin, M.]]
[[Category: Overduin, M.]]
[[Category: Yamabhai, M.]]
[[Category: Yamabhai, M.]]
[[Category: calcium binding]]
[[Category: Calcium binding]]
[[Category: complex]]
[[Category: Complex]]
[[Category: ef-hand]]
[[Category: Ef-hand]]
[[Category: eh domain]]
[[Category: Eh domain]]
[[Category: npf]]
[[Category: Npf]]
[[Category: signaling domain]]
[[Category: Signaling domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:01:42 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:17:59 2008''

Revision as of 16:01, 2 May 2008

File:1f8h.gif

Template:STRUCTURE 1f8h

STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 IN COMPLEX WITH PTGSSSTNPFR


OverviewOverview

Eps15 homology (EH) domains are protein interaction modules that recognize Asn-Pro-Phe (NPF) motifs in their biological ligands to mediate critical events during endocytosis and signal transduction. To elucidate the structural basis of the EH-NPF interaction, the solution structures of two EH-NPF complexes were solved using NMR spectroscopy. The first complex contains a peptide representing the Hrb C-terminal NPFL motif; the second contains a peptide in which an Arg residue substitutes the C-terminal Leu. The NPF residues are almost completely embedded in a hydrophobic pocket on the EH domain surface and the backbone of NPFX adopts a conformation reminiscent of the Asx-Pro type I beta-turn motif. The residue directly following NPF is crucial for recognition and is required to complete the beta-turn. Five amino acids on the EH surface mediate specific recognition of this residue through hydrophobic and electrostatic contacts. The complexes explain the selectivity of the second EH domain of Eps15 for NPF over DPF motifs and reveal a critical aromatic interaction that provides a conserved anchor for the recognition of FW, WW, SWG and HTF ligands by other EH domains.

About this StructureAbout this Structure

1F8H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Molecular mechanism of NPF recognition by EH domains., de Beer T, Hoofnagle AN, Enmon JL, Bowers RC, Yamabhai M, Kay BK, Overduin M, Nat Struct Biol. 2000 Nov;7(11):1018-22. PMID:11062555 Page seeded by OCA on Fri May 2 16:01:42 2008

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