Preparation of crystals for characterizing the Grb7 SH2 domain before and after complex formation with a bicyclic peptide antagonist

Nigus Dessalew Ambaye, Menachem Joseph Gunzburg, Daouda A K Traore, Mark Pasqualino Del Borgo, Patrick Perlmutter, Matthew Charles James Wilce, Jacqueline Anne Wilce

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4 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)182 - 186
Number of pages5
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number2
Publication statusPublished - 2014

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