Peptides identify the critical hotspots involved in the biological activation of the insulin receptor

81Citations
Citations of this article
47Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

We used phage display to generate surrogate peptides that define the hotspots involved in protein-protein interaction between insulin and the insulin receptor. All of the peptides competed for insulin binding and had affinity constants in the high nanomolar to low micromolar range. Based on competition studies, peptides were grouped into non-overlapping Sites 1, 2, or 3. Some Site 1 peptides were able to activate the tyrosine kinase activity of the insulin receptor and act as agonists in the insulin-dependent fat cell assay, suggesting that Site 1 marks the hotspot involved in insulin-induced activation of the insulin receptor. On the other hand, Site 2 and 3 peptides were found to act as antagonists in the phosphorylation and fat cell assays. These data show that a peptide display can be used to define the molecular architecture of a receptor and to identify the critical regions required for biological activity in a site-directed manner.

Cite

CITATION STYLE

APA

Pillutla, R. C., Hsiao, K. C., Beasley, J. R., Brandt, J., Østergaard, S., Hansen, P. H., … Goldstein, N. I. (2002). Peptides identify the critical hotspots involved in the biological activation of the insulin receptor. Journal of Biological Chemistry, 277(25), 22590–22594. https://doi.org/10.1074/jbc.M202119200

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free