Docking studies of Clo or Can with PRMT5 (IMAGE)
Caption
Images show that (a) in SAM-bound condition, Clo bound to a site distinct from SAM on PRMT5, (b) in apo condition (in the absence of SAM), several binding residues for Clo with PRMT5 overlapped with SAM, suggesting that Clo could block PRMT5 activity by interfering with binding several similar residues as SAM.
Credit
Drs. Özlem Demir and Rommie E. Amaro
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License
CC BY-NC-ND