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Figure 5.
Figure 5 Point mutations in the Amph2 SH3 domain. (A) Structure
of Amph2 SH3 showing positions of key mutated residues, coloured
according to type. Hydrophobic residues are coloured green and
acidic residues in magenta. The longer n-Src loop which is
unique to the amphiphysins (the DAPS) that is exchanged for the
shorter homologous loop from Grb2 NSH3 is coloured blue. (B)
Effect of point mutations in GST Amph2 SH3 domain on its ability
to bind dynamin. (C) Interaction between Amph2 SH3 and dynamin
is sensitive to pH. Binding to wild-type is maximal at pH 7.0,
but rapidly declines as pH is either increased or decreased.
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