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. 1991 Jan 1;88(1):249–252. doi: 10.1073/pnas.88.1.249

A model for the quaternary structure of human placental insulin receptor deduced from electron microscopy.

K Christiansen 1, J Tranum-Jensen 1, J Carlsen 1, J Vinten 1
PMCID: PMC50787  PMID: 1986371

Abstract

Electrophoretically pure and functionally intact human placental insulin receptor was studied by electron microscopy with negative-staining techniques. The quaternary structure of the detergent-solubilized receptor was determined. The receptor had the shape of a letter T approximately 24 nm in height and 18 nm in width with a thickness of the stem and the crossbar of 3-4 nm. No consistent change in ultrastructure of the receptor could be detected after the addition of insulin alone or insulin and Mn2+/Mg2+/ATP. After partial reduction of the alpha 2 beta 2 heterotetrameric receptor into alpha beta heterodimers, the electron micrographs showed a clear reduction in average size of the molecule with disappearance of the T profiles characteristic of the alpha 2 beta 2 heterotetramers. By incubation of the heterodimers in a phosphorylation medium containing insulin, a reassociation to molecules with molecular weights of the alpha 2 beta 2 heterotetramer took place judged from SDS/PAGE. Electron microscopy showed that the molecule formed larger aggregates, and only a few solitary T-shaped copies were seen.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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