Figure 2 - full size

 

Figure 2.
Figure 2. Binding of pYVNV to TEF1W Src SH2(a) Stereo ribbon diagram of TEF1W Src SH2 complexed with the phosphopeptide SpYVNVQN. A σ[A] weighted 2F[obs] − F[c] electron density map at 1.0 σ is contoured around the phosphopeptide.(b) In the same orientation as (a) but with the SH2 domain represented as van der Waals spheres and the phosphopeptide as a ball-and-stick model. The pYVNV peptide is shown with bonds in orange, Src with atoms in white except residue TrpEF1 (in magenta), TyrβD5 (in green), IleβE4 (in peach), LysβD6 (in pink), and ArgαA2 and ArgβB5 (in cyan).(c) Superposition of the TEF1W Src SH2 complexed with the SpYVNVQN structure onto the native Grb2 SH2 complexed with KRFpYVNV. For clarity, only the phosphopeptide residues resolved in both structures are shown (SpYVNV for Src TEF1W, FpYVNV for Grb2). Src TEF1W is in lighter shades (yellow, cyan, light green, and magenta for Src, the peptide, TyrβD5, and TrpEF1, respectively) while Grb2 is in darker shades (orange, blue, dark green, and purple for Grb2, the peptide, PheβD6, and TrpEF1, respectively). Coordinates for Grb2 SH2 were taken from the crystal structure of Rahuel et al. ([25]) (RCSB ID code 1tze).

The above figure is reprinted by permission from Cell Press: Mol Cell (2000, 5, 1043-1049) copyright 2000.