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PDBsum entry 1gfd
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Adaptor protein containing sh2 and sh3
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PDB id
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1gfd
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References listed in PDB file
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Key reference
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Title
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Solution structure and ligand-Binding site of the carboxy-Terminal sh3 domain of grb2.
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Authors
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D.Kohda,
H.Terasawa,
S.Ichikawa,
K.Ogura,
H.Hatanaka,
V.Mandiyan,
A.Ullrich,
J.Schlessinger,
F.Inagaki.
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Ref.
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Structure, 1994,
2,
1029-1040.
[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
95%.
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Abstract
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BACKGROUND: Growth factor receptor-bound protein 2 (GRB2) is an adaptor protein
with three Src homology (SH) domains in the order SH3-SH2-SH3. Both SH3 domains
of GRB2 are necessary for interaction with the protein Son of sevenless (Sos),
which acts as a Ras activator. Thus, GRB2 mediates signal transduction from
growth factor receptors to Ras and is thought to be a key molecule in signal
transduction. RESULTS: The three-dimensional structure of the carboxy-terminal
SH3 domain of GRB2 (GRB2 C-SH3) was determined by NMR spectroscopy. The SH3
structure consists of six beta-strands arranged in two beta-sheets that are
packed together perpendicularly with two additional beta-strands forming the
third beta-sheet. GRB2 C-SH3 is very similar to SH3 domains from other proteins.
The binding site of the ligand peptide (VPP-PVPPRRR) derived from the Sos
protein was mapped on the GRB2 C-SH3 domain indirectly using 1H and 15N chemical
shift changes, and directly using several intermolecular nuclear Overhauser
effects. CONCLUSIONS: Despite the structural similarity among the known SH3
domains, the sequence alignment and the secondary structure assignments differ.
We therefore propose a standard description of the SH3 structures to facilitate
comparison of individual SH3 domains, based on their three-dimensional
structures. The binding site of the ligand peptide on GRB2 C-SH3 is in good
agreement with those found in other SH3 domains.
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Figure 6.
Figure 6. Schematic representation of GRB2 C–SH3 and
other SH3 domains. The βI–sheet is drawn in red, the
βII–sheet is in blue, the βIII–sheet is in green, the
3[10]–helix is in magenta, and the rest is in white. PI3K SH3
was drawn using the coordinates of bovine PI3K. The ribbon
diagrams in Fig 6 and Figure8 were generated using the program
MOLSCRIPT [52]. Figure 6. Schematic representation of
GRB2 C–SH3 and other SH3 domains. The βI–sheet is drawn in
red, the βII–sheet is in blue, the βIII–sheet is in green,
the 3[10]–helix is in magenta, and the rest is in white. PI3K
SH3 was drawn using the coordinates of bovine PI3K. The ribbon
diagrams in Fig 6 and [3]Figure8 were generated using the
program MOLSCRIPT [[4]52].
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Figure 8.
Figure 8. The overlay of the backbone atoms of the 38 residues
found in regions of the conserved secondary structures, The SH3
structures superimposed are GRB2 C–SH3 (white), PLCγ
(yellow), spectrin (red), Fyn (purple), Src (green) and bovine
PI3K (blue). The structures are in the same orientation as in
Figure 2a. Figure 8. The overlay of the backbone atoms of the
38 residues found in regions of the conserved secondary
structures, The SH3 structures superimposed are GRB2 C–SH3
(white), PLCγ (yellow), spectrin (red), Fyn (purple), Src
(green) and bovine PI3K (blue). The structures are in the same
orientation as in [3]Figure 2a.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(1994,
2,
1029-1040)
copyright 1994.
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