Structure and evolution of insulins: Implications for receptor binding
- 1 May 1992
- Vol. 14 (5) , 325-331
- https://doi.org/10.1002/bies.950140507
Abstract
Insulin is a member of a family of hormones, growth factors and neuropeptides which are found in both vertebrates and invertebrates. A common ‘insulin fold’ is probably adopted by all family members. Although the specificities of receptor binding are different, there is possibility of co‐evolution of polypeptides and their receptors.Keywords
This publication has 44 references indexed in Scilit:
- X-ray structure of human relaxin at 1.5 pComparison to insulin and implications for receptor binding determinantsJournal of Molecular Biology, 1991
- X-ray analysis of the single chain B29-A1 peptide-linked insulin moleculeJournal of Molecular Biology, 1991
- Comparative 2D NMR studies of human insulin and despentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognitionBiochemistry, 1991
- On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptorsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Prothoracicotropic hormone has an insulin‐like tertiary structureFEBS Letters, 1987
- Transmission of conformational change in insulinNature, 1983
- Insulin's structural behavior and its relation to activityBiopolymers, 1983
- Primary structure of human insulin‐like growth factor IIFEBS Letters, 1978
- Primary structure of the B-chain of porcine relaxinBiochemical and Biophysical Research Communications, 1977
- Receptor-binding region of insulinNature, 1976