Figure 2. Structure of the SNT-1 PTB Domain/hFGFR1 Complex.

(A) Stereoview of the backbone atom superposition of the final 20 NMR-derived structures of the complex. The figure shows the SNT-1 PTB domain residues 18–116 and the hFGFR1 peptide residues 411–430. The terminal residues, which are structurally disordered, are omitted for clarity. For the final 20 structures, the root-mean-square deviations (rmsd) of the backbone and all heavy atoms for protein residues 18–116 are 0.74 ± 0.16 Å and 1.46 ± 0.16 Å, respectively. The corresponding rmsd for the protein secondary- structural regions (protein residues 19–24, 35–40, 45–49, 52–57, 63–68, 71–76, 85–90, 94–107, and 111–115) are 0.40 ± 0.05 A and 0.88 ± 0.05 A, respectively. The rmsd of the backbone and all heavy atoms for the hFGFR1 peptide (residues 412–430) are 0.56 ± 0.10 Å and 1.25 ± 0.15 Å, respectively.

(B) Ribbons (Carson, 1991) depiction of the averaged minimized NMR structure of the SNT-1 PTB domain/hFGFR1 complex. The orientation of (B) is as shown in (A).

(C) Ribbon diagram of the SNT-1 PTB domain structure from the top of the protein, which is rotated ~90° from the orientation in (B).

(D) Molecular surface representation of the SNT-1 PTB domain structure calculated in GRASP (Nicholls et al., 1993). The protein is color coded by surface curvature, and the color gradient from green to dark gray reflects decreasing solvent exposure. The hFGFR1 peptide molecule is shown as a ball-and-stick representation color coded by atom type.