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Figure 3.
Figure 3. P47^phox Constitutes a Novel Mode of SH3 Domain
Ligand Interactions(A) Intramolecular interactions between the
sequence R[296]GAPPRRSS[304] and the tandem SH3 domains. The
molecular surfaces of SH3[A] and SH3[B] are shown in blue-gray
and green-gray, respectively. Residues 296–303 are depicted in
stick format; Ser304 has been omitted for clarity. SH3-domain
residues involved in the intramolecular interaction are
indicated by their residue number.(B) Schematic representation
of the interactions between the RGAPPRRSS-motif and the tandem
SH3 domains. The figure was drawn with LIGPLOT (Wallace et al.,
1995). Residues of the polybasic core are shown in blue and
residues of the two SH3 domains in orange. Hydrogen bonds are
depicted as black lines with the bond distances indicated in
Å and hydrophobic interactions are shown as green
(SH3-domains) and blue (polybasic peptide) rays.
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