NDLI: Preliminary crystallographic characterization of the Grb2 SH2 domain in complex with a FAK-derived phosphotyrosyl peptide.

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Preliminary crystallographic characterization of the Grb2 SH2 domain in complex with a FAK-derived phosphotyrosyl peptide.

Content Provider	Europe PMC
Author	Chen, Hsiao-Hsin Chen, Cuei-Wen Chang, Yu-Yung Shen, Tang-Long Hsu, Chun-Hua
Copyright Year	2010
Description	Crystals of the Grb2 SH2 domain in complex with a phosphotyrosyl peptide corresponding to residues 921–930 of focal adhesion kinase (FAK) have been obtained using the sitting-drop vapour-diffusion technique. Data have been collected to 2.49 Å resolution. 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 P3121, with unit-cell parameters a = b = 102.7, c = 127.6 Å, α = β = 90.0, γ = 120.0°. A diffraction data set was collected from a flash-cooled crystal at 100 K to 2.49 Å resolution using synchrotron radiation. Structure determination by molecular replacement and analysis of the detailed structure of the complex are currently in progress.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2815691&blobtype=pdf
Volume Number	66
PubMed Central reference number	PMC2815691
Issue Number	Pt 2
Issue Number	pt 2
PubMed reference number	20124721
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications [Acta Crystallogr Sect F Struct Biol Cryst Commun]
e-ISSN	17443091
DOI	10.1107/s1744309109053184
Language	English
Publisher	International Union of Crystallography
Publisher Date	2010-01-28
Access Restriction	Open
Rights License	© International Union of Crystallography 2010
Subject Keyword	Grb2 SH2 domain FAK
Content Type	Text
Resource Type	Article
Subject	Biochemistry Condensed Matter Physics Genetics Biophysics Structural Biology

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