Figure 2.
Dimeric conformation of GPVI in the crystal. (A) Structure of the GPVI dimer in the asymmetric unit. (B) Electrostatic potential of GPVI mapped onto the surface of each GPVI protomer, shown in an “open-book” view. Residues contributing to the dimer interface on each protomer have been outlined in yellow. The potential map has been contoured from –100 to +100 kT. (C) Stereoview of a superposition of the dimers formed by GPVI D2 (blue/green) and the CD3ϵγ heterodimer42 (purple/yellow). For clarity, only those β-strands in the continuous β-sheet are shown as ribbons; all others are shown as coils.
