Figure 5
From: Allosteric conformational changes of human HBV core protein transform its assembly
Structural features of HBc dimers in tube, capsid and sheet-like ensemble. (a) Structural models of dimers in tube (left), capsid (middle) and sheet-like ensemble (right), displayed as space-filled models with hydrophilic and hydrophobic residues rendered blue and red respectively, or (b) depictured as grey ribbon models with hydrophobic residues in helix α5 and helix α1 displayed as red sticks. (c) The trimers of dimers in the unit cell/asymmetric unit of HBc tube, capsid and sheet-like ensemble are displayed as grey ribbon models with hydrophobic residues in helix α5 and helix α1 displayed as red sticks. The three inter-dimer distances within the trimer of dimers of tube, capsid and sheet-like ensemble are labelled.
