Kumaran Sangaralingam, Grucza Richard A, Waksman Gabriel
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, Saint Louis, MO 63110, USA.
Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14828-33. doi: 10.1073/pnas.2432867100. Epub 2003 Dec 1.
Conformational flexibility is important for protein function. However, information on the range of conformations accessible to macromolecules in the unbound state is often difficult to obtain. By using the model system of the tandem Src homology 2 domain (i.e., two adjacent Src homology 2 domains) of the Syk kinase, we report a method combining calorimetric and crystallographic measurements that reveals the preexistence of a conformational equilibrium in the unbound state, and that shows that this equilibrium is crucial for function.
构象灵活性对蛋白质功能很重要。然而，关于未结合状态下大分子可及构象范围的信息往往难以获得。通过使用Syk激酶的串联Src同源2结构域（即两个相邻的Src同源2结构域）的模型系统，我们报告了一种结合量热法和晶体学测量的方法，该方法揭示了未结合状态下构象平衡的预先存在，并表明这种平衡对功能至关重要。
