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. 2021 Aug 31;13(17):4392. doi: 10.3390/cancers13174392

Figure 3.

Figure 3

Inhibitors binding to the A-site cleft impede the binding of the aa-tRNA during elongation. (a) Overview of the inhibitors that bind to the A-site cleft. All compounds would sterically clash with the incoming charged acylated A-site tRNA, thus impairing accommodation of the following amino acid within the pocket and therefore halting the elongation phase of translation. Anisomycin (ANI) in lemon (PDB: 4U3M), agelastatin A (AglA) in cyan (PDB: 5MEI), deoxyvalenol in fuchsia (PDB: 4U53), haemanthamine (HAE) in blue (PDB: 5ON6), homoharringtonine (HHT) in brown (PDB: 4U4Q), lycorine (LYC) in light blue (PDB: 4U4U), nagilactone C in aquamarine (PDB: 4U52), narciclasine (NAR) in green forest (PDB: 4U51), T2-toxin in purple (PDB: 4U6F) and verrucarin A (PDB: 4U50) in blue navy; (b) zoom-in and details of interaction for HHT within the A-site cleft. Proximal rRNA residues are shown as sticks; (c) zoom-in and details of interaction for HAE within the A-site cleft; (d) zoom-in and details of interaction for ANI within the A-site cleft; (e) zoom-in and details of interaction for AglA within the A-site cleft. The rRNA residues that adopt different conformations upon binding of the inhibitors, A2404 and U2875, are shown for clarity. The peculiar halogen–π interaction established between the pyrimidine ring of U2875 and the bromine atom of AglA is also highlighted.