Three-dimensional structure of the hepatitis B core antigen particle truncated at residue 154  

作　　者：LIU ShuYu HE Jian LI KunPeng DAI AGuang CAI ChangJie ZHANG JingQiang 

机构地区：[1]State Key Laboratory of Biocontrol, Life Sciences School, Sun Yat-sen University, Guangzhou 510275, China [2]Guangzhou East Campus Lab Center, Sun Yat-sen University, Guangzhou 510006, China [3]Third Affiliated Hospital of Sun Yat-sen University, Guangzhou 510080, China

出　　处：《Science China(Life Sciences)》2011年第2期171-174,共4页中国科学（生命科学英文版）

基　　金：supported by special funds of the National Natural Science Foundation of China (Grant No. 10274106)

摘　　要：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.The three-dimensional structure of recombinant hepatitis B core antigen(HBcAg) particles truncated at residue 154(HBcAg-154) was determined to 7.8 ? 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.

关 键 词：HBcAg-154 particle CAPSID RNA CRYOEM 

分 类 号：Q71[生物学—分子生物学] S859.797[农业科学—临床兽医学]