1prl: Difference between revisions

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TWO BINDING ORIENTATIONS FOR PEPTIDES TO SRC SH3 DOMAIN: DEVELOPMENT OF A GENERAL MODEL FOR SH3-LIGAND INTERACTIONS

OverviewOverview

Solution structures of two Src homology 3 (SH3) domain-ligand complexes have been determined by nuclear magnetic resonance. Each complex consists of the SH3 domain and a nine-residue proline-rich peptide selected from a large library of ligands prepared by combinatorial synthesis. The bound ligands adopt a left-handed polyproline type II (PPII) helix, although the amino to carboxyl directionalities of their helices are opposite. The peptide orientation is determined by a salt bridge formed by the terminal arginine residues of the ligands and the conserved aspartate-99 of the SH3 domain. Residues at positions 3, 4, 6, and 7 of both peptides also intercalate into the ligand-binding site; however, the respective proline and nonproline residues show exchanged binding positions in the two complexes. These structural results led to a model for the interactions of SH3 domains with proline-rich peptides that can be used to predict critical residues in complexes of unknown structure. The model was used to identify correctly both the binding orientation and the contact and noncontact residues of a peptide derived from the nucleotide exchange factor Sos in association with the amino-terminal SH3 domain of the adaptor protein Grb2.

About this StructureAbout this Structure

1PRL is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions., Feng S, Chen JK, Yu H, Simon JA, Schreiber SL, Science. 1994 Nov 18;266(5188):1241-7. PMID:7526465

Page seeded by OCA on Thu Feb 21 14:31:46 2008

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OCA

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-[[Image:1prl.gif|left|200px]]<br /><applet load="1prl" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1prl.gif|left|200px]]<br /><applet load="1prl" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1prl" />
 '''TWO BINDING ORIENTATIONS FOR PEPTIDES TO SRC SH3 DOMAIN: DEVELOPMENT OF A GENERAL MODEL FOR SH3-LIGAND INTERACTIONS'''<br />
 ==Overview==
-Solution structures of two Src homology 3 (SH3) domain-ligand complexes, have been determined by nuclear magnetic resonance. Each complex consists, of the SH3 domain and a nine-residue proline-rich peptide selected from a, large library of ligands prepared by combinatorial synthesis. The bound, ligands adopt a left-handed polyproline type II (PPII) helix, although the, amino to carboxyl directionalities of their helices are opposite. The, peptide orientation is determined by a salt bridge formed by the terminal, arginine residues of the ligands and the conserved aspartate-99 of the SH3, domain. Residues at positions 3, 4, 6, and 7 of both peptides also, intercalate into the ligand-binding site; however, the respective proline, and nonproline residues show exchanged binding positions in the two, complexes. These structural results led to a model for the interactions of, SH3 domains with proline-rich peptides that can be used to predict, critical residues in complexes of unknown structure. The model was used to, identify correctly both the binding orientation and the contact and, noncontact residues of a peptide derived from the nucleotide exchange, factor Sos in association with the amino-terminal SH3 domain of the, adaptor protein Grb2.
+Solution structures of two Src homology 3 (SH3) domain-ligand complexes have been determined by nuclear magnetic resonance. Each complex consists of the SH3 domain and a nine-residue proline-rich peptide selected from a large library of ligands prepared by combinatorial synthesis. The bound ligands adopt a left-handed polyproline type II (PPII) helix, although the amino to carboxyl directionalities of their helices are opposite. The peptide orientation is determined by a salt bridge formed by the terminal arginine residues of the ligands and the conserved aspartate-99 of the SH3 domain. Residues at positions 3, 4, 6, and 7 of both peptides also intercalate into the ligand-binding site; however, the respective proline and nonproline residues show exchanged binding positions in the two complexes. These structural results led to a model for the interactions of SH3 domains with proline-rich peptides that can be used to predict critical residues in complexes of unknown structure. The model was used to identify correctly both the binding orientation and the contact and noncontact residues of a peptide derived from the nucleotide exchange factor Sos in association with the amino-terminal SH3 domain of the adaptor protein Grb2.
 ==About this Structure==
-PRL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PRL OCA].
+PRL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRL OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Gallus gallus]]
 [[Category: Single protein]]
-[[Category: Chen, J.K.]]
+[[Category: Chen, J K.]]
 [[Category: Feng, S.]]
-[[Category: Schreiber, S.L.]]
+[[Category: Schreiber, S L.]]
-[[Category: Simon, J.A.]]
+[[Category: Simon, J A.]]
 [[Category: Yu, H.]]
 [[Category: complex (signal transduction/peptide)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:03:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:46 2008''