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Figure 3.
Interactions between p110α and p85 nSH2. (A) Ribbon diagram
of nSH2, helical, and kinase domains determined from the
structure reported in this work. (B) The same ribbon diagram as
in A but showing the position of the PDGFR phosphopeptide (gray)
modeled as in PDB ID code 2IUI, at the interface between nSH2
and the helical domain. The loop of the helical domain occupies
nearly the same position as the phosphopeptide, so their
occurrence is mutually exclusive. (C) The phosphopeptide is
predicted to disrupt the interaction between the positively
charged nSH2 surface (shaded blue) and the negatively charged
helical domain residues. The phosphopeptide is shown in gray,
with its phosphotyrosine in stick and ball representation and
the phosphate shaded red. The boxed region shows that the side
chain of Glu-542 occupies the space usually occupied by the
phosphate of the peptide's phosphotyrosine residue.
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