Fig. 3: Alignment of Pf20S and human 20S proteasomes. | Nature Communications

Fig. 3: Alignment of Pf20S and human 20S proteasomes.

From: Structures revealing mechanisms of resistance and collateral sensitivity of Plasmodium falciparum to proteasome inhibitors

Fig. 3

a The β2 binding pocket of Pf20S-TDI-8304 was aligned with those of human c-20S (PDB ID 5LF3) and i-20S (PDB ID 7AWE) and shown separately. b The β5 binding pocket of Pf20S-TDI-8304 was aligned with those of c-20S and i-20S and shown separately. The clash sites are indicated magenta circles with white crosses. The β5 Pro126 of c-20S clashes with the pyrrolidinone of TDI-8304, and the β5 Pro126 and Cys48 of i-20S clash with pyrrolidinone and P2-P4 tether of TDI-8304, respectively. In panels a and b, the water-mediated H-bonds between TDI-8304 and Pf20S were not shown, to provide a fair comparison with the computationally docked TDI-8304 binding poses in the human 20S particles. c EM map of the c-20S complexed with TDI-8304 at 2.04 Å overall resolution. The inhibitor densities (magenta) were found only in the β5, but not in any other sites. d EM density of the TDI-8304 in a β5 site. e Interactions of TDI-8304 with the human β5 site.

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