Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules

Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules

The NADase SARM1 (sterile alpha and TIR motif containing 1) is a key executioner of axon degeneration and a therapeutic target for several neurodegenerative conditions. We show that a potent SARM1 inhibitor undergoes base exchange with the nicotinamide moiety of nicotinamide adenine dinucleotide (NA...

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Main Authors: Adams, S.E (Author), Bosanac, T. (Author), Brearley, A. (Author), Brillault, L. (Author), Cunnea, K. (Author), DiAntonio, A. (Author), Furrer, M. (Author), Gu, W. (Author), Hughes, R.O (Author), Kerry, P.S (Author), Kobe, B. (Author), Krauss, R. (Author), Landsberg, M.J (Author), Luo, Z. (Author), Mao, X. (Author), Masic, V. (Author), Milbrandt, J. (Author), Mosaiab, T. (Author), Nanson, J.D (Author), Rose, F. (Author), Saikot, F.K (Author), Sasaki, Y. (Author), Shi, Y. (Author), Vasquez, E. (Author), Ve, T. (Author)
Format: Article
Language:English
Published: Cell Press 2022
Subjects:
allosteric activator
ARM domain
base exchange
cryo-EM
NADase
orthosteric inhibitor
TIR domain
X-ray crystallography
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