The three-dimensional structure of recombinant hepatitis B core antigen（HBcAg） particles truncated at residue 154（HBcAg-154） was determined to 7.8 A resolution by cryo-electron microscopy（cryoEM） and computer re...The three-dimensional structure of recombinant hepatitis B core antigen（HBcAg） particles truncated at residue 154（HBcAg-154） was determined to 7.8 A resolution by cryo-electron microscopy（cryoEM） and computer reconstruction.The capsid of HBcAg-154 is mainly constituted by α-helical folds,highly similar to that of HBcAg-149.The C-terminal region between residues 155 and 183 of the core protein is more crucial to the encapsidation of RNA,and the short C-terminal tail of HBcAg-154 results in a nearly empty capsid.展开更多
基金supported by special funds of the National Natural Science Foundation of China (Grant No. 10274106)
文摘The three-dimensional structure of recombinant hepatitis B core antigen（HBcAg） particles truncated at residue 154（HBcAg-154） was determined to 7.8 A resolution by cryo-electron microscopy（cryoEM） and computer reconstruction.The capsid of HBcAg-154 is mainly constituted by α-helical folds,highly similar to that of HBcAg-149.The C-terminal region between residues 155 and 183 of the core protein is more crucial to the encapsidation of RNA,and the short C-terminal tail of HBcAg-154 results in a nearly empty capsid.
