1f8h: Difference between revisions

Revision as of 13:36, 21 February 2008

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 with as ligand. 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 Thu Feb 21 12:36:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1f8h.gif|left|200px]]<br />
+[[Image:1f8h.gif|left|200px]]<br /><applet load="1f8h" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1f8h" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1f8h" />
 '''STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 IN COMPLEX WITH PTGSSSTNPFR'''<br />
 ==Overview==
-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.
+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 Structure==
-F8H 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]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F8H OCA].
+F8H 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 <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8H OCA].
 ==Reference==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Beer, T.De.]]
+[[Category: Beer, T De.]]
-[[Category: Bowers, R.C.]]
+[[Category: Bowers, R C.]]
-[[Category: Enmon, J.L.]]
+[[Category: Enmon, J L.]]
-[[Category: Hoofnagle, A.N.]]
+[[Category: Hoofnagle, A N.]]
-[[Category: Kay, B.K.]]
+[[Category: Kay, B K.]]
 [[Category: Overduin, M.]]
 [[Category: Yamabhai, M.]]
@@ Line 29: / Line 28: @@
 [[Category: signaling domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:50:06 2007''
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