Figure 4 - full size

 

Figure 4.
Figure 4. Electrostatic surface potentials of (A) TSP TSR2, (B) F-spondin TSR1, and (C) F-spondin TSR4. Each domain is shown from two sides, which are rotated by 180° around a vertical axis relative to each other. For the F-spondin TSR domains, the structures with the lowest total energy are shown. Charged residues are labeled. Red labels identify residues that are conserved in the sequence alignment and have similar positions on the surfaces of all three domains. The charged side-chains D496, E497, and D498 in F-spondin TSR1 and D625, K632, K642, E646, D649, and D653 in F-spondin TSR4 have larger than 2 Å side-chain RMSDs.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 64, 665-672) copyright 2006.