Mechanism of MEK1 phosphorylation by the N-terminal acidic motif mediated asymmetric BRAF dimer
Yasushi Kondo, Judith Notbohm, Ignacio Navas Camacho, Gabriela Nagy‐Davidescu, Thomas J. Mason, Jonas Mühle, J. Standfuss, Tina Perica
The paper presents the first X-ray structure of an NtA-mediated asymmetric BRAF dimer bound to MEK1, showing it is a catalytically active state, not an intermediate in BRAF activation.
Molecular Cell · Jul 21, 2026Peer-reviewedBiochemistry