Abstract
The three-dimensional structure of recombinant hepatitis B core antigen (HBcAg) particles truncated at residue 154 (HBcAg-154) was determined to 7.8 Å 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.
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Liu, S., He, J., Li, K. et al. Three-dimensional structure of the hepatitis B core antigen particle truncated at residue 154. Sci. China Life Sci. 54, 171–174 (2011). https://doi.org/10.1007/s11427-010-4098-x
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DOI: https://doi.org/10.1007/s11427-010-4098-x