Fig. 3 in Bat coronaviruses related to SARS-CoV-2 and infectious for human cells

Fig. 3 | Dynamicsof thebindingof hACE2 to bat-sarbecovirus-borne RBDs andinsightintothestructureofthecomplex. a, Biolayerinterferometry (BLI) bindinganalysis of thehACE2 peptidasedomaintoimmobilized BANAL-52/103,BANAL-236 or SARS-CoV-2 RBDs.Black linescorrespondto aglobalfitof thedatausinga 1:1 bindingmodel.b, Frequencyofformationof saltbridgesclosetothe RBD–ACE2 interface (fromlefttoright:D30/K417, E35/ K493, D38/K493, K31/E35 and D38/K353) duringthecourseof the MD simulations.Theanalysiswasperformedforninedifferent MDsimulations (threereplicatesforeachcomplex) ofhACE2 incomplexwith RBDs from SARS-CoV-2 (SARS-CoV-2.1,SARS-CoV-2.2 and SARS-CoV-2.3, shadesof green), BANAL-236 (BANAL 236-CoV.1, BANAL 236-CoV.2 and BANAL 236-CoV.3,shadesof red) and BANAL-52/103 (BANAL 52/103-CoV.1, BANAL 52/103-CoV.2 and BANAL 52/103-CoV.3, shadesofblue). c, Ribbon representationsof thecrystalstructuresof thehACE2 peptidase domain (cyan) incomplexwith SARS-CoV-2 (PDB 6M0J) or BANAL-236 (this study,PDB 7PKI) RBDs (pink). Blackarrowsintheoverallstructuresindicatethestructural differencebetweenthetwocomplexesatthelevelofhelix H4. The magnificationsshowthemaininteractionsinthe ACE2–RBD interfaces. Residuesinthereceptor-bindingmotif alteredbetween SARS-CoV-2 and BANAL-236 arehighlighted withcolouredoutlines.Numbers 1, 2 and 3 indicate thethreemainclustersof interactionsbetweenhACE2 and RBDs.