Figure 6
From: Allosteric conformational changes of human HBV core protein transform its assembly
Schematic model of HBc assembly controlled by allosteric conformational changes. In wild-type, the HBc dimer is in the assembly-active (HBcAct) conformation and the HBc dimers first assemble into trimer of dimers, in which the interactions between dimers are weak, hence the trimer is thermodynamically unstable therefore the assembly proceeds further to a large, closed ensemble, the capsid (upper panel). BAY41-4109 induces a conformational change of HBc dimer and renders it into an aberrant conformation (HBcAbb), the HBc dimers first assemble into trimer of dimers, in which the interactions between dimers are even weaker, hence the trimer is thermodynamically unstable therefore the assembly proceeds further to an even large ensemble, the tube (lower panel). The binding of BAY41-4109 to the preformed capsid can also change the conformation of HBc dimer from HBcAct to HBcAbb and destabilize the capsid, which may render the capsid to dissociate into trimers of dimers or dimers; the trimers of dimers or dimers then re-associate to assemble into a tube.
