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- W2801604220 endingPage "870.e7" @default.
- W2801604220 startingPage "857" @default.
- W2801604220 abstract "Epidermal growth factor receptor (EGFR) interacts through its extracellular domain with seven different growth factors. These factors induce different structures within the cytoplasmic juxtamembrane (JM) segment of the dimeric receptor and propagate different growth factor-dependent signals to the cell interior. How this process occurs is unknown. Here we apply diverse experimental and computational tools to show that growth factor identity is encoded by the EGFR transmembrane (TM) helix into discrete helix dimer populations that differ in both cross-location and cross-angle. Helix dimers with smaller cross-angles at multiple cross locations are decoded to induce an EGF-type coiled coil in the adjacent JM, whereas helix dimers with larger cross-angles at fewer cross locations induce the TGF-α-type coiled coil. We propose an updated model for how conformational coupling across multiple EGFR domains results in growth factor-specific information transfer, and demonstrate that this model applies to both EGFR and the related receptor ErbB2." @default.
- W2801604220 created "2018-05-17" @default.
- W2801604220 creator A5044272398 @default.
- W2801604220 creator A5047960543 @default.
- W2801604220 creator A5055114409 @default.
- W2801604220 creator A5067830024 @default.
- W2801604220 date "2018-07-01" @default.
- W2801604220 modified "2023-10-16" @default.
- W2801604220 title "Mechanism of Allosteric Coupling into and through the Plasma Membrane by EGFR" @default.
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- W2801604220 doi "https://doi.org/10.1016/j.chembiol.2018.04.005" @default.
- W2801604220 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6054568" @default.
- W2801604220 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29731426" @default.
- W2801604220 hasPublicationYear "2018" @default.
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