Figure 5 - full size


Figure 5.
Figure 5. Tertiary Interactions between Nef[core] and Fyn(R96I) SH3 Domain(A) Molecular surface of Nef, showing the binding site for the isoleucine side chain of the SH3 domain.(B) Comparison of the interactions in the two complexes in the crystal. The polypeptide backbones of Nef and the SH3 domain are shown as green and blue tubes, respectively. Side chains of Nef are shown in pink and in yellow (displayed under their respective molecular surfaces). SH3 side chains are shown in red. Hydrogen bonding interactions are shown as dashed lines. Hydrogen bonds to backbone positions are indicated by the placement of white circles along the backbone ribbon. For clarity, the side chain of Ile-96 is not shown, and instead the Cα position of this residue is indicated with a red circle. The structure on the left is the complex that is the focus of the major part of the discussion in the text. The structure on the right is that of the second independent complex in the crystal. Note the slight change in the relative orientation of the Nef and SH3 components of the complex (see text). The side chain of Asp-86 forms a hydrogen bond with Thr-97 in the RT loop of the second complex. For clarity, this interaction is not shown.

The above figure is reprinted by permission from Cell Press: Cell (1996, 85, 931-942) copyright 1996.