title: Three-dimensional structure of the hepatitis B core antigen particle truncated at residue 154.
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.
authors.affiliation: State Key Laboratory of Biocontrol, Life Sciences School, Sun Yat-sen University, Guangzhou 510275, China.
authors.forename: ShuYu
authors.initials: S
authors.lastname: Liu
authors.forename: Jian
authors.initials: J
authors.lastname: He
authors.forename: KunPeng
authors.initials: K
authors.lastname: Li
authors.forename: Aguang
authors.initials: A
authors.lastname: Dai
authors.forename: ChangJie
authors.initials: C
authors.lastname: Cai
authors.forename: JingQiang
authors.initials: J
authors.lastname: Zhang
mesh_terms: D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry; D020285:Cryoelectron Microscopy / Q000379:methods*; D006512:Hepatitis B Core Antigens / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure*; D006515:Hepatitis B virus / Q000378:metabolism; D006801:Humans; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D006512:Hepatitis B Core Antigens