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• W1979244942 abstract "The primary hormone-binding surface of the insulin receptor spans one face of the N-terminal β-helix of the α-subunit (the L1 domain) and an α-helix in its C-terminal segment (αCT). Crystallographic analysis of the free ectodomain has defined a contiguous dimer-related motif in which the αCT α-helix packs against L1 β-strands 2 and 3. To relate structure to function, we exploited expanded genetic-code technology to insert photo-activatable probes at key sites in L1 and αCT. The pattern of αCT-mediated photo–cross-linking within the free and bound receptor is in accord with the crystal structure and prior mutagenesis. Surprisingly, L1 photo-probes in β-strands 2 and 3, predicted to be shielded by αCT, efficiently cross-link to insulin. Furthermore, anomalous mutations were identified on neighboring surfaces of αCT and insulin that impair hormone-dependent activation of the intracellular receptor tyrosine kinase (contained within the transmembrane β-subunit) disproportionately to their effects on insulin binding. Taken together, these results suggest that αCT, in addition to its hormone-recognition role, provides a signaling element in the mechanism of receptor activation." @default.
• W1979244942 created "2016-06-24" @default.
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• W1979244942 date "2012-06-26" @default.
• W1979244942 modified "2023-10-11" @default.
• W1979244942 title "α-Helical element at the hormone-binding surface of the insulin receptor functions as a signaling element to activate its tyrosine kinase" @default.
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• W1979244942 doi "https://doi.org/10.1073/pnas.1205681109" @default.
• W1979244942 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3396503" @default.
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