Slide 3 of 10

Previous

Next

Home

To identify the binding site for the monoclonal IgG, we used a panel of thrombin mutants provided by Craig Gibbs and Manuel Tsiang.  In each of these mutants, one or several residues on the surface of thrombin were replaced by alanine.  We found that mutations of arginine-101, argining-233, or lysine-236 decrease the apparent affinity of thrombin for the monoclonal IgG.  These residues lie next to each other in exosite II and have been implicated in binding to heparin and prothrombin fragment 2.  The locations of exosite I and the active site are also shown in this figure.