Similar but different: ligand-induced activation of the insulin and epidermal growth factor receptor families
- Author(s)
- Ward, CW; Lawrence, MC;
- Details
- Publication Year 2012-06,Volume 22,Issue #3,Page 360-366
- Journal Title
- CURRENT OPINION IN STRUCTURAL BIOLOGY
- Publication Type
- Journal Article
- Abstract
- The insulin and epidermal growth factor receptor families are among the most intensively studied proteins in biology. They are closely related members of the receptor tyrosine kinase superfamily and deregulated signaling by members of either receptor family has been implicated in the progression of a variety of cancers. These receptors have thus emerged as validated therapeutic targets for the development of anti-tumour agents. Recent studies have revealed detail of the ligand-binding sites in the insulin receptor family, as well as detail of conformational change upon ligand binding in the epidermal growth factor receptor family. Taken together, these findings and further data relating to kinase activation highlight the fact that while the receptor families share common structural elements, the structural detail of their functioning is remarkably different.
- Publisher
- CURRENT BIOLOGY LTD
- Keywords
- FACTOR-I-RECEPTOR; 1ST 3 DOMAINS; CRYSTAL-STRUCTURE; EGF RECEPTOR; EXTRACELLULAR REGION; KINASE DOMAIN; NEGATIVE COOPERATIVITY; JUXTAMEMBRANE REGION; STRUCTURAL-ANALYSIS; ECTODOMAIN REVEALS
- Research Division(s)
- Structural Biology
- Publisher's Version
- https://doi.org/10.1016/j.sbi.2012.03.014
- Terms of Use/Rights Notice
- Crown copyright © 2012 Published by Elsevier Ltd. All rights reserved.
Creation Date: 2012-06-01 12:00:00