Conformational states of the insulin receptor.
Conformational states of the insulin receptor.
复制标题
胰岛素受体的构象状态。
DOI：
10.1016/s0006-291x(88)80024-x
复制
发表时间：
1988
影响因子：
3.1
通讯作者：
Kohanski,RA
中科院分区：
文献类型：
--
作者：
Schenker,E;Kohanski,RA
Insulin binding to theα-subunit of the purified insulin receptor changed the interaction betweenβ-subunits. This conformational change was demonstrated after labeling the receptor'sβ-subunit by autophosphorylation in the absence of insulin, and then crosslinking the subunits to each other with bis(sulfosuccinimidyl)suberate. The covalent oligomers were resolved by reduction and denaturing gel electrophoresis. Insulin increased the rate of crosslinking, especially the formation ofβ-βdimers. These results support a conformational change following insulin binding, and may reflect the insulin-induced activation of autophosphorylation.
