Table of Contents
Cells, Volume 6, Issue 2 (June 2017)
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Cover Story (view full-size image) Ligand binding rearranges conformation of the extracellular domains of an EGFR dimer from tethered [...] Read more. Ligand binding rearranges conformation of the extracellular domains of an EGFR dimer from tethered to untethered. This rearrangement induces a rotation/twist of the transmembrane domain of the receptor parallel to the plane of the cell membrane, resulting in the reorientation of the intracellular kinase domain dimer from a symmetric inactive configuration (left) to an asymmetric active form (right). Oncogenic mutations, shown by red balls, may also induce the asymmetric active form of the kinase dimer without ligand binding. View this paper