1f8h: Difference between revisions
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'''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 IN COMPLEX WITH PTGSSSTNPFR''' | {{Structure | ||
|PDB= 1f8h |SIZE=350|CAPTION= <scene name='initialview01'>1f8h</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 IN COMPLEX WITH PTGSSSTNPFR''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F8H is a [ | 1F8H 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=1F8H OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11062555 11062555] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signaling domain]] | [[Category: signaling domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:05:51 2008'' | ||
Revision as of 12:05, 20 March 2008
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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
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