Related Experiment Video
Updated: Feb 16, 2026

Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay
Published on: July 15, 2025
Conformational states of the insulin receptor
1Department of Biochemistry, Mount Sinai School of Medicine, New York, New York 10029.
Abstract:
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 convalent 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.
Related Concept Videos
Insulin: The Receptor and Signaling Pathways
The Two-State Receptor Model
The binding affinity of a drug determines its interaction with...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Insulin Secretory Vesicles

