Human growth factor receptor-bound protein 7 (Grb7) is an adapter protein involved in cell growth, migration and proliferation. It is now recognized that Grb7 is an emerging therapeutic target in specific cancer subtypes. Recently, the discovery of a bicyclic peptide inhibitor that targets the Grb7 SH2 domain, named G7-B1, was reported. In an attempt to probe the foundation of its interaction with Grb7, the crystallization and preliminary data collection of both the apo and G7-B1-bound forms of the Grb7 SH2 domain are reported here. Diffraction-quality crystals were obtained using the hanging-drop vapour-diffusion method. After several rounds of microseeding, crystals of the apo Grb7 SH2 domain were obtained that diffracted to 1.8 A resolution, while those of the G7-B1-Grb7 SH2 domain complex diffracted to 2.2 A resolution. The apo Grb7 SH2 domain crystallized in the trigonal space group P63, whereas the G7-B1-Grb7 SH2 domain complex crystallized in the monoclinic space group P21. The experimental aspects of crystallization, crystal optimization and data collection and the preliminary data are reported.
|Pages (from-to)||182 - 186|
|Number of pages||5|
|Journal||Acta Crystallographica. Section F: Structural Biology Communications|
|Publication status||Published - 2014|
Ambaye, N. D., Gunzburg, M. J., Traore, D. A. K., Del Borgo, M. P., Perlmutter, P., Wilce, M. C. J., & Wilce, J. A. (2014). Preparation of crystals for characterizing the Grb7 SH2 domain before and after complex formation with a bicyclic peptide antagonist. Acta Crystallographica. Section F: Structural Biology Communications, 70(2), 182 - 186. https://doi.org/10.1107/S2053230X13033414