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Structure and evolution of insulins: implications for receptor binding.

J Murray-Rust¹, A N McLeod, T L Blundell

¹Laboratory of Molecular Biology, Birkbeck College, London, UK.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology

|May 1, 1992

Summary

Insulin and related peptides share a common structural fold, suggesting evolutionary links. This conserved structure may indicate co-evolution between these molecules and their respective receptors across species.

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Area of Science:

Biochemistry
Evolutionary Biology
Molecular Endocrinology

Background:

Insulin belongs to a diverse family of signaling molecules including growth factors and neuropeptides.
These molecules are conserved across both vertebrate and invertebrate species.
A shared structural motif, the 'insulin fold', is likely present in all family members.

Purpose of the Study:

To explore the evolutionary conservation of the 'insulin fold' across different species.
To investigate the potential for co-evolution between insulin-like peptides and their receptors.

Main Methods:

Comparative structural analysis of insulin family members.
Bioinformatic analysis of peptide and receptor sequences.
Review of existing literature on insulin-like signaling pathways.

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Main Results:

A common 'insulin fold' is highly conserved among insulin, growth factors, and neuropeptides.
Receptor binding specificities vary significantly within the family.
Evidence suggests a potential for co-evolution between these peptides and their receptors.

Conclusions:

The conserved 'insulin fold' highlights a fundamental structural basis for this signaling family.
Despite differing receptor specificities, the shared ancestry implies coordinated evolutionary trajectories between peptides and receptors.