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- Crystallization and preliminary diffraction analysis of the T2I.L262F double mutant form of SHP2
- Hye Seon Lee; Bonsu Ku; Ho Chul Shin; Seung Jun Kim
- Bibliographic Citation
- Biodesign, vol. 10, no. 4, pp. 69-72
- Publication Year
- The enzymatic activity of SHP2, whose dysregulation causes malfunctions in diverse cellular signaling, is controlled by the autoinhibitory association between its N-SH2 and phosphatase domains. Various SHP2 genetic mutations, which impair the interaction between the two domains, have been identified to cause RAS-MAPK pathway-associated diseases. In this study, SHP2 containing Noonan syndrome-associated T2I and L262F double mutations was targeted for crystallization. The recombinant protein was prepared using an Escherichia coli expression system, purified using Ni-NTA affinity and size exclusion chromatographies, and then subjected for crystallization. X-ray data diffracted to 3.0 A resolution were collected and used for preliminary diffraction analysis. The unit cell parameters of the crystals belonging to the P21 space group were a = 45.4 A, b = 215.0 A, c = 55.6 A, and β = 95.7°. The asymmetric unit contains two molecules with a solvent content of 40.7% and a Matthews coefficient of 2.07 A3/Da.
- Korea Soc-Assoc-Inst
- Appears in Collections:
- Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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