In:
Acta Crystallographica Section F Structural Biology Communications, International Union of Crystallography (IUCr), Vol. 70, No. 2 ( 2014-02-01), p. 182-186
Abstract:
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 Å resolution, while those of the G7-B1–Grb7 SH2 domain complex diffracted to 2.2 Å resolution. The apo Grb7 SH2 domain crystallized in the trigonal space group P 6 3 , whereas the G7-B1–Grb7 SH2 domain complex crystallized in the monoclinic space group P 2 1 . The experimental aspects of crystallization, crystal optimization and data collection and the preliminary data are reported.
Type of Medium:
Online Resource
ISSN:
2053-230X
DOI:
10.1107/S2053230X13033414
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2014
detail.hit.zdb_id:
2175956-X
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