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Updated: Jun 6, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Three-dimensional structure of the hepatitis B core antigen particle truncated at residue 154
ShuYu Liu1, Jian He, KunPeng Li
1State Key Laboratory of Biocontrol, Life Sciences School, Sun Yat-sen University, Guangzhou 510275, China.
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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