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Figure 3.
Figure 3. Comparison of PLCg1-SH3 in free and SLP-76-bound
forms. (a) Superposition of the polypeptide chain of unbound
PLCg1-SH3 (gold) onto that of PLCg1-SH3 in the PLCg1-SH3/SLP-76
complex (cyan). The SLP-76 peptide is drawn in ball-and-stick
representation. The arrow points to the region where the two
structures deviate most. (b) Close-up view of the rearrangement
of the n-Src loop of PLCg1-SH3 following peptide binding.
Glycine residues are represented by their carbonyl oxygen atoms.
(c) Adjustments in the PLCg1-SH3 binding site upon ligation of
SLP-76 peptide. Free PLCg1-SH3 was superposed on SLP-76-bound
PLCg1-SH3. The view is looking down on the binding groove. The
SLP-76 peptide and the rest of the SH3 structure are omitted for
clarity. Only residues contacting the ligand are shown. Glycine
residues are represented by their carbonyl oxygen atoms. Dual
conformations were observed for the side-chains Gln805 and
Arg806 in the PLCg1-SH3/SLP-76 complex.
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