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PDBsum entry 1hsq
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Phosphoric diester hydrolase
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PDB id
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1hsq
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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 of the sh3 domain of phospholipase c-Gamma.
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Authors
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D.Kohda,
H.Hatanaka,
M.Odaka,
V.Mandiyan,
A.Ullrich,
J.Schlessinger,
F.Inagaki.
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Ref.
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Cell, 1993,
72,
953-960.
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PubMed id
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Abstract
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SH3 (Src homology 3) domains are found in many signaling proteins and appear to
function as binding modules for cytoplasmic target proteins. The solution
structure of the SH3 domain of human phospholipase C-gamma (PLC-gamma) was
determined by two-dimensional 1H NMR analysis. This SH3 domain is composed of
eight antiparallel beta strands consisting of two successive "Greek key" motifs,
which form a barrel-like structure. The conserved aliphatic and aromatic
residues form a hydrophobic pocket on the molecular surface, and the conserved
carboxylic residues are localized to the periphery. The hydrophobic pocket may
serve as a binding site for target proteins. Analysis of the slowly exchanging
amide protons by NMR measurements indicates that despite containing a high
content of beta structure, the SH3 domain of PLC-gamma is flexible.
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Secondary reference #1
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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 have
been manually determined.
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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
reproduced from the cited reference
with permission from Cell Press
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