Conformational states of the insulin receptor
Schenker, E.; Kohanski, R.A.
Biochemical and Biophysical Research Communications 157(1): 140-145
1988
ISSN/ISBN: 0006-291X PMID: 3058124 Document Number: 322417
Insulin binding to the .alpha.-subunit of the purified insulin receptor changed the interaction between .beta.-subunits. This conformational change was demonstrated after labeling the receptor's .beta.-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 of .beta.-.beta. dimers. These results support a conformational change following insulin binding, and may reflect the insulin-induced activation of autophosphorylation.