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Figure 2.
Figure 2. A Comparison of Peptide Binding Surfaces between
the Gads and c-Src SH3 Domains(A) Surface representation of the
Gads SH3-C domain – SLP-76 peptide complex. Areas of positive
and negative charges are shown in blue and red, respectively.
Residues in the peptides that occupy the four binding pockets on
the SH3 domain surface (identified in dotted circles) are
labeled in black. Residue Glu275 of the protein, which encloses
the second pocket, is labeled in red.(B) Surface representation
of the c-Src SH3 domain – APP12 peptide complex (adapted from
Feng et al., 1995). APP12 is a dodecapeptide that binds with
high affinity to the c-Src SH3 domain (Kd = 1.2 μM). Since the
last four residues of the peptide do not contribute
significantly to SH3 binding (Feng et al., 1995), only the first
eight residues of the peptide (A^1PPLPPRN^8) are shown for
clarity. As in (A), key residues in peptide APP12 that engage
the three binding pockets (identified as dotted circles) on the
c-Src SH3 domain are labeled.
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