Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 17, Issue 6, Pages 699-705Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2007.07.007
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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.
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