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Crystallization and preliminary diffraction analysis of dual specificity phosphatase 13a
민희경,전태진,위천화,김명빈,류성언 한국구조생물학회 2018 Biodesign Vol.6 No.1
Dual specificity phosphatases (DUSPs) include MAP kinase phosphatases and atypical dual specificity phosphatases,and mediate cell growth and differentiation. They are considered as drug targets against cancers, diabetes, immunediseases, and neuronal diseases. Two different DUSPs, DUSP13a and DUSP13b are coded in one gene (DUSP13) whosealternative splicing results in two sequence-related proteins with different target specificities. The crystal structure ofDUSP13b showed a canonical DUSP fold. However, the structure of DUSP13a has not been determined yet. To understandstructural mechanism of distinctive target specificities of sequence-related DUSPs, we prepared diffraction-quality crystalsof DUSP13a. Cysteine residues in DUSP13a gene were mutated to serine or alanine to prevent cysteine oxidation. Fromthe stabilized protein, we were able to grow good crystals that diffracted to 1.7 Å resolution. The preliminary diffractionanalysis revealed that the crystal is in the space group P21 with unit cell parameters of a = 40.04 Å, b = 89.34 Å, c = 45.90 Å,α = 90.00°, β = 89.87° and γ = 90.00°.