Back

Identification of a small molecule antagonist for the Tudor domain of SMN

Liu, Y.; Iqbal, A.; Li, W.; Ni, Z.; Zhao, D. Y.; Abraham, K. J.; Tempel, W.; Guo, X.; Zhou, M.; Brown, P. J.; Qin, S.; Mekhail, K.; Greenblatt, J. F.; Min, J.

2019-11-11 biochemistry
10.1101/829689 bioRxiv
Show abstract

Survival of motor neuron (SMN), a Tudor-domain-containing protein, plays an important role in diverse biological pathways via recognition of symmetrically dimethylated arginine (Rme2s) on proteins by its Tudor domain, and deficiency of SMN leads to the motor neuron degenerative disease spinal muscular atrophy (SMA). Here we report a potent and selective antagonist with a 4-iminopyridine scaffold targeting the Tudor domain of SMN. Our structural and mutagenesis studies indicate that the sandwich stacking interactions of SMN and compound 1 play a critical role in selective binding to SMN. Various on-target engagement assays support that compound 1 recognizes SMN specifically in a cellular context. In cell studies display that the SMN antagonist prevent the interaction of SMN with R1810me2s of DNA-directed RNA polymerase II subunit POLR2A and results in transcription termination and R-loop accumulation, mimicking depletion of SMN. Thus, in addition to the antisense, RNAi and CRISPR/Cas9 techniques, the potent SMN antagonist could be used as an efficient tool in understanding the biological functions of SMN and molecular etiology in SMA.

Matching journals

The top 8 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.