Crystal structure of DD dimer interface showing simulated γGly309Asp mutation.

Because of the asymmetric nature of the D:D interface, the simulated γAsp309 residue has 2 different sets of potential interactions. γAsp309 in molecule 1 causes steric repulsion of γAla279 and γTyr280 in molecule 2 and γAsp309 in molecule 2 causes electrostatic repulsion of γGlu323 in molecule 1. Asterisks indicate new Asp side chains. The model was created using Swiss-PdbViewer. The inset shows 2 fibrin monomers interacting, with the D:D interface blackened.