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

Sci China Life Sci. 2011 Feb;54(2):171-4. doi: 10.1007/s11427-010-4098-x. Epub 2010 Nov 19.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Capsid / chemistry
  • Cryoelectron Microscopy / methods*
  • Hepatitis B Core Antigens / chemistry*
  • Hepatitis B Core Antigens / genetics
  • Hepatitis B Core Antigens / ultrastructure*
  • Hepatitis B virus / metabolism
  • Humans
  • Image Processing, Computer-Assisted
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary*

Substances

  • Hepatitis B Core Antigens