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. 2021 Mar 22;16(11):1697–1716. doi: 10.1002/cmdc.202100039

Figure 6.

Figure 6

Natural compounds targeting the Gα‐accessory protein interface. A) Modification of Gαs by cholera toxin (CTX). CTX transfers the ADP‐ribose element from nicotinamide adenine dinucleotide (NAD+) to ArgG.hfs2.2 of Gαs, thereby inhibiting GTP hydrolysis. B) Modification of Gαi by P. multocida toxin (PMT). PMT catalyzes the deamidation of GlnG.s3h2.3 to GluG.s3h2.3 and thus inhibits GTP hydrolysis. C) Crystal structures (gray) of cholera toxin (CTX, PDB ID: 1XTC [213] ), heat‐labile enterotoxin (HLT, PDB ID: 1LTS [207] ), P. multocida toxin (PMT, PDB ID: 2EC5 [214] ) and the P. asymbiotica protein toxin (PaTox) glycosyltransferase domain (PDB ID: 4MIX [212] ) in complex with UDP‐GlcNAc (violet).