Structure-function relationships in insulin
- 1 June 1981
- journal article
- research article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 1 (6) , 485-495
- https://doi.org/10.1007/bf01121582
Abstract
A new interpretation of structure-function relationships in the insulin molecule is presented. Negative cooperativity is postulated to arise from a dimerization event occurring between two receptor-bound molecules. The receptor-binding surface of insulin can necessarily not involve residues involved in dimerization as has been generally accepted. Support for this interpretation is based on published data.This publication has 45 references indexed in Scilit:
- Multiple Redox Forms of the Insulin Receptor in Native Liver MembranesDiabetes, 1980
- Photoreactive insulin analogues used to characterise the insulin receptorBiochemical and Biophysical Research Communications, 1980
- The Insulin Receptor in Vertebrates Is Functionally More Conserved during Evolution than Insulin ItselfEndocrinology, 1979
- Kinetics of Cooperative BindingPublished by Springer Nature ,1979
- Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulinNature, 1978
- Purification and properties of insulin receptors from rat liver membranesBiochemical and Biophysical Research Communications, 1977
- The insulin receptor of the turkey erythrocyte characterization of the membrane-bound receptorBiochimica et Biophysica Acta (BBA) - Biomembranes, 1976
- Receptor-binding region of insulinNature, 1976
- Binding of insuling and other hormones to non-receptor materials: Saturability, specificity and apparent “negative cooperativity”Biochemical and Biophysical Research Communications, 1975
- Insulin interactions with its receptors: Experimental evidence for negative cooperativityBiochemical and Biophysical Research Communications, 1973