How ligand binds to the type 1 insulin-like growth factor receptor

Journal: Nature Communications

Published: 2018-02-26

DOI: 10.1038/s41467-018-03219-7

Affiliations: 9

Authors: 10

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Research Highlight

A crystal-clear view of an insulin-related receptor

© LAGUNA DESIGN/Science Photo Library/Getty

© LAGUNA DESIGN/Science Photo Library/Getty

The crystallization of a receptor involved in the growth and differentiation of cells could lead to new insights that will help to develop anti-cancer drugs.

Malfunctioning ‘human type 1 insulin-like growth factor receptor’ (IGF-1R) has been implicated in the growth and spread of cancer. By crystalizing the normally functioning receptor, researchers are closer to understanding its atomic structure and how the receptor interacts with growth factor hormones. When these hormones bind with complementary sites on IGF-1R, which are present on the surface of human cells, IGF-1R sends signals to direct pathways responsible for cell growth and differentiation.

Scientists at Flinders University, South Australia, and colleagues crystalized the interacting part of the receptor both separately and in a complex with a hormone called insulin-like growth factor. This allowed them to examine the receptor’s atomic structure and see how the hormone binds to it.

Further research is needed to understand how this interaction changes the receptor’s structure such that it sends signals. Such knowledge could help the development of anti-cancer drugs targeting the receptor.

Supported content

  1. Nature Communications 9, 821 (2018). doi: 10.1038/s41467-018-03219-7
Institutions FC
Walter and Eliza Hall Institute of Medical Research (WEHI), Australia 0.50
College of Medicine and Public Health, Flinders University, Australia 0.20
Department of Medical Biology, UniMelb, Australia 0.10
Eli Lilly and Company, United States of America (USA) 0.10
de Duve Institute, UCL, Belgium 0.05
Novo Nordisk A/S, Denmark 0.03
De Meyts R&D Consulting SPRLU, Belgium 0.03

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