Abstract
Growth factor receptor-bound protein 2 (Grb2) is an adaptor protein with a single SH2 domain that specifically binds to focal adhesion kinase (FAK) when residue Tyr925 of FAK is phosphorylated. The Grb2-FAK interaction is associated with cellular integrin-activated signal transduction events leading to the activation of the Ras-MAPK pathway. Crystals of the Grb2 SH2 domain in complex with a phosphopeptide corresponding to residues 921-930 of FAK have been obtained using the sitting-drop vapour-diffusion technique. The crystals belonged to space group P3(1)21, with unit-cell parameters a = b = 102.7, c = 127.6 A, alpha = beta = 90.0, gamma = 120.0 degrees . A diffraction data set was collected from a flash-cooled crystal at 100 K to 2.49 A resolution using synchrotron radiation. Structure determination by molecular replacement and analysis of the detailed structure of the complex are currently in progress.