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. 2010 Dec 1;66(Pt 12):1640-3.
doi: 10.1107/S1744309110041850. Epub 2010 Nov 26.

Preparation and crystallization of the Grb7 SH2 domain in complex with the G7-18NATE nonphosphorylated cyclic inhibitor peptide

Min Y Yap  1 , Matthew C J Wilce, Daniel J Clayton, Patrick Perlmutter, Marie-Isabel Aguilar, Jacqueline A Wilce
Affiliations

Preparation and crystallization of the Grb7 SH2 domain in complex with the G7-18NATE nonphosphorylated cyclic inhibitor peptide

Min Y Yap et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

Grb7 is an adapter protein that is involved in signalling pathways that mediate eukaryotic cell proliferation and migration. Its overexpression in several cancer types has implicated it in cancer progression and led to the development of the G7-18NATE cyclic peptide inhibitor. Here, the preparation of crystals of G7-18NATE in complex with its Grb7 SH2 domain target is reported. Crystals of the complex were grown by the hanging-drop vapour-diffusion method using PEG 3350 as the precipitant at room temperature. X-ray diffraction data were collected from crystals to 2.4 Å resolution using synchrotron X-ray radiation at 100 K. The diffraction was consistent with space group P2(1), with unit-cell parameters a=52.7, b=79.1, c=54.7 Å, α=γ=90.0, β=104.4°. The structure of the G7-18NATE peptide in complex with its target will facilitate the rational development of Grb7-targeted cancer therapeutics.

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Figures

Figure 1
Figure 1
Crystals of the Grb7 SH2–G7-18NATE complex of approximately 0.01 × 0.06 × 0.1 mm in size.
Figure 2
Figure 2
A representative diffraction image acquired from a Grb7 SH2–G7-18NATE complex crystal.
See this image and copyright information in PMC

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