期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 67, 期 -, 页码 336-339出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110053728
关键词
Csk-homologous kinase; Src-homology 2 domains; enzyme inhibition; Src-family protein tyrosine kinases; cancer; small-angle X-ray scattering
资金
- Australian National Health and Medical Research Council (NHMRC) [509115]
- Australian Institute of Nuclear Science and Engineering (AINSE) [09137]
- C. R. Roper Fellowship
The C-terminal Src kinase (Csk) and Csk-homologous kinase (CHK) are endogenous inhibitors of the proto-oncogenic Src family of protein tyrosine kinases (SFKs). Phosphotyrosyl peptide binding to their Src-homology 2 (SH2) domains activates Csk and CHK, enhancing their ability to suppress SFK signalling; however, the detailed mechanistic basis of this activation event is unclear. The CHK SH2 was expressed in Escherichia coli and the purified protein was characterized as monomeric by synchrotron small-angle X-ray scattering in-line with size-exclusion chromatography. The CHK SH2 crystallized in 0.2 M sodium bromide, 0.1 M bis-Tris propane pH 6.5 and 20% polyethylene glycol 3350 and the best crystals diffracted to similar to 1.6 A resolution. The crystals belonged to space group P2, with unit-cell parameters a = 25.8, b = 34.6, c = 63.2 A, beta = 99.4 degrees.
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