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PDBsum entry 1qwe
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Complex (signal transduction/peptide)
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PDB id
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1qwe
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Specific interactions outside the proline-Rich core of two classes of src homology 3 ligands.
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Authors
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S.Feng,
C.Kasahara,
R.J.Rickles,
S.L.Schreiber.
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Ref.
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Proc Natl Acad Sci U S A, 1995,
92,
12408-12415.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
89%.
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Abstract
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Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands
and selected from biased phage display libraries were used to investigate
interactions between a specificity pocket in the Src SH3 domain and ligant
residues flanking the proline-rich core. The solution structures of c-Src SH3
complexed with these peptides were solved by NMR. In addition to proline-rich,
polyproline type II helix-forming core, the class I and II ligands each
possesses a flanking sequence that occupies a large pocket between the RT and
n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how
the two classes of SH3 ligands exploit a specificity pocket on the receptor
differently to increase binding affinity and specificity.
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Secondary reference #1
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Title
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Structural basis for the binding of proline-Rich peptides to sh3 domains.
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Authors
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H.Yu,
J.K.Chen,
S.Feng,
D.C.Dalgarno,
A.W.Brauer,
S.L.Schreiber.
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Ref.
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Cell, 1994,
76,
933-945.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Two binding orientations for peptides to the src sh3 domain: development of a general model for sh3-Ligand interactions.
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Authors
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S.Feng,
J.K.Chen,
H.Yu,
J.A.Simon,
S.L.Schreiber.
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Ref.
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Science, 1994,
266,
1241-1247.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Solution structure of the sh3 domain of src and identification of its ligand-Binding site.
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Authors
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H.Yu,
M.K.Rosen,
T.B.Shin,
C.Seidel-Dugan,
J.S.Brugge,
S.L.Schreiber.
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Ref.
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Science, 1992,
258,
1665-1668.
[DOI no: ]
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PubMed id
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