Figure 6

G7-18NATE binding surface on the Grb7 SH2 domain. (a) An overlay of the ¹⁵N, ¹H-HSQC spectra of Grb7 SH2 alone (black) and in the presence of two molar equivalents of G7-18NATE (red). The insert shows changes to signals in the boxed region of the HSQC spectrum over the course of the titration. The ratio of G7-18NATE to Grb7 SH2 is 0:1, 1:4, 1:2, 3:4, 1:1 and 2:1 in the black, red, blue, orange, purple and green spectra respectively. (b) The rate of change of peak volume over the titration series versus Grb7 SH2 domain residue number. The broken line indicates the mean rate of change. Residues that exhibited rates of change greater than this value are coloured according to their location in the Grb7 SH2 domain structure. (c) Surface representation of the Grb7 SH2 domain with residues affected by G7-18NATE binding coloured. The majority of residues cluster onto either the phosphopeptide binding surface (red) or the dimerisation interface (green). Residues shown in blue were also affected by G7-18NATE binding but do not cluster on one surface. The two images are related by a 90° rotation about the horizontal axis of the page.