Lambright D G, Noel J P, Hamm H E, Sigler P B
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510.
Nature. 1994 Jun 23;369(6482):621-8. doi: 10.1038/369621a0.
The 1.8 A crystal structure of transducin alpha.GDP, when compared to that of the activated complex with GTP-gamma S, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein alpha-subunit. Structural changes initiated by direct contacts with the terminal phosphate of GTP propagate to regions that have been implicated in effector activation. The changes are distinct from those observed in other members of the GTPase superfamily.
与转导素α.GDP的1.8埃晶体结构相比，转导素α.GDP与GTP-γS形成的活化复合物的晶体结构揭示了异源三聚体G蛋白α亚基激活时发生的构象变化的本质。由与GTP末端磷酸基团直接接触引发的结构变化会传播到与效应器激活有关的区域。这些变化与在GTP酶超家族其他成员中观察到的变化不同。
