Preliminary crystallographic characterization of the Grb2 SH2 domain in complex with a FAK-derived phosphotyrosyl peptide.
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.
Chen
Hsiao Hsin
HH
Department of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan.
Chen
Cuei Wen
CW
Chang
Yu Yung
YY
Shen
Tang Long
TL
Hsu
Chun Hua
CH
D003461:Crystallography; D051417:Focal Adhesion Kinase 1 / Q000737:chemistry* / Q000378:metabolism; D051380:GRB2 Adaptor Protein / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D014961:X-Ray Diffraction; D018909:src Homology Domains
D051380:GRB2 Adaptor Protein; C495948:GRB2 protein, human; D010455:Peptides; D051417:Focal Adhesion Kinase 1; C496050:PTK2 protein, human