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Figure 5.
Figure 5. Solution structures of the (a) and (b)
Bin1C(SH3)/c-Myc(55-68) complex and (c) and (d) the Bin1+12A
intramolecular complex. (a) An ensemble of 20 superimposed
NMR-derived structures of Bin1C(SH3) bound to the synthetic
peptide c-Myc(55-68) (shown in red) and (c) ensemble structures
of the 213 residue Bin1C+12A intramolecular complex. For
clarity, only residues 305–311 (RKGPPVP) (green) and the SH3
domain of Bin1C+12A intramolecular complex are shown. The
orientation of the proline-rich peptides is different in the two
structures, reflecting the difference in the locations of the
positively charged residues within each peptide sequence. The
locations of the n-Src, RT, and distal loops of the SH3 domain
are shown in (a). (b) and (d) Molecular surface representations
of the Bin1C(SH3)/c-Myc(55-68) complex and the Bin1+12A
intramolecular complex with positive and negative electrostatic
potential colored blue and red, respectively. The bound peptide
sequences (c-Myc and +12A) are shown above. The two positively
charged residues of each SH3 binding region are shown in green.
The conserved c-Myc residues, Thr58 and Ser62, are shown in
light blue and yellow, respectively. See the text for
discussion.
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