Identification of a Novel Allosteric Binding Site for RORgt Inhibitors Descriptor: (1S)-4-{1-[2-chloro-6-(trifluoromethyl)benzoyl]-4-fluoro-1H-indazol-3-yl}-1-methylcyclohex-3-ene-1-carboxylic acid, G
The ribonuclease H (RNase H) domain on the p66 monomer of HIV-1 reverse transcriptase enzyme has become a target for inhibition. The active site is one potential binding site, but other RNase H sites
Serine/threonine-protein kinase PAK1 complexed with a dibenzodiazepine: identification of an allosteric site on PAK1 Descriptor: 2,8-difluoro-11-(4-methylpiperazin-1-yl)-5H-dibenzo[b,e][1,4]diazepine,
Allostery is involved in innumerable biological processes and plays a fundamental role in human disease. Thus, the exploration of allosteric modulation is crucial for research on biological mechanisms