莫洛尼鼠白血病病毒跨膜蛋白之间的同源相互作用。
Homomeric interactions between transmembrane proteins of Moloney murine leukemia virus.
作者信息
Li X, McDermott B, Yuan B, Goff S P
机构信息
Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA.
出版信息
J Virol. 1996 Feb;70(2):1266-70. doi: 10.1128/JVI.70.2.1266-1270.1996.
Abstract
We have studied homomeric interactions between transmembrane proteins (TM) of the Moloney murine leukemia virus envelope using the Saccharomyces cerevisiae two-hybrid system. TM interacts strongly with itself but not with various control proteins. Deletional and mutational analyses indicated that the putative leucine zipper motif in the extracellular domain of TM is essential and sufficient to mediate the binding. The first three repeats of the leucine zipper-like motif are the most important in mediating the interaction. The TM-TM interaction detected in this system may play a role in several stages of viral replication.
摘要
我们利用酿酒酵母双杂交系统研究了莫洛尼鼠白血病病毒包膜跨膜蛋白（TM）之间的同聚相互作用。TM与自身强烈相互作用，但与各种对照蛋白不相互作用。缺失和突变分析表明，TM胞外结构域中假定的亮氨酸拉链基序对于介导结合是必不可少且足够的。亮氨酸拉链样基序的前三个重复在介导相互作用中最为重要。在该系统中检测到的TM-TM相互作用可能在病毒复制的几个阶段发挥作用。
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