Insulin receptor structure and its implications for the IGF-1 receptor
- Author(s)
- Lawrence, MC; McKern, NM; Ward, CW;
- Details
- Publication Year 2007-12,Volume 17,Issue #6,Page 699-705
- Journal Title
- CURRENT OPINION IN STRUCTURAL BIOLOGY
- Publication Type
- Journal Article
- Abstract
- The insulin receptor (isoforms IR-A and IR-B) and the type-1 insulin-like growth factor receptor (IGF-1R) are homologous, multi-domain tyrosine kinases that bind insulin and IGF-1 with differing specificity. IR is involved in metabolic regulation and IGF-1R in normal growth and development. IR-A also binds IGF-2 with an affinity comparable to IGF-1 R and, like the latter, is implicated in a range of cancers. The recent structure of the IR ectodomain dimer explains many features of ligand-receptor binding and provides insight into the structure of the intact ligand-binding site in both receptors. The structures of the L1-CR-L2 fragments of IR and IGF-1 R reveal major differences in the regions that govern ligand specificity. The IR ectodomain Xray structure raises doubts about that obtained by STEM reconstruction.
- Publisher
- CURRENT BIOLOGY LTD
- Keywords
- GROWTH-FACTOR RECEPTOR; DIABETES-ASSOCIATED MUTATIONS; PHOTO-CROSS-LINKING; 1ST 3 DOMAINS; LIGAND-BINDING; I-RECEPTOR; CRYSTAL-STRUCTURE; HYBRID RECEPTORS; B-CHAIN; ACTIVATION
- Publisher's Version
- https://doi.org/10.1016/j.sbi.2007.07.007
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2007-12-01 12:00:00