Three-dimensional structure of the hepatitis B core antigen particle truncated at residue 154 |
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| Authors: | ShuYu Liu Jian He KunPeng Li AGuang Dai ChangJie Cai JingQiang Zhang |
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| Institution: | (1) Fysica van complexe systemen, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands;(2) Department of Biochemistry, Centre for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, 221 00 Lund, Sweden; |
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| 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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