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2ZTN

Hepatitis E virus ORF2 (Genotype 3)

Summary for 2ZTN
Entry DOI10.2210/pdb2ztn/pdb
DescriptorCapsid protein (1 entity in total)
Functional Keywordshev, virus
Biological sourceHepatitis E virus
Total number of polymer chains1
Total formula weight51610.40
Authors
Yamashita, T.,Unno, H.,Mori, Y.,Li, T.C.,Takeda, N.,Matsuura, Y. (deposition date: 2008-10-08, release date: 2009-08-25, Last modification date: 2024-03-13)
Primary citationYamashita, T.,Mori, Y.,Miyazaki, N.,Cheng, R.H.,Yoshimura, M.,Unno, H.,Shima, R.,Moriishi, K.,Tsukihara, T.,Li, T.C.,Takeda, N.,Miyamura, T.,Matsuura, Y.
Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure
Proc.Natl.Acad.Sci.USA, 106:12986-12991, 2009
Cited by
PubMed Abstract: Hepatitis E virus (HEV) is a causative agent of acute hepatitis. The crystal structure of HEV-like particles (HEV-LP) consisting of capsid protein was determined at 3.5-A resolution. The capsid protein exhibited a quite different folding at the protruding and middle domains from the members of the families of Caliciviridae and Tombusviridae, while the shell domain shared the common folding. Tyr-288 at the 5-fold axis plays key roles in the assembly of HEV-LP, and aromatic amino acid residues are well conserved among the structurally related viruses. Mutational analyses indicated that the protruding domain is involved in the binding to the cells susceptive to HEV infection and has some neutralization epitopes. These structural and biological findings are important for understanding the molecular mechanisms of assembly and entry of HEV and also provide clues in the development of preventive and prophylactic measures for hepatitis E.
PubMed: 19620712
DOI: 10.1073/pnas.0903699106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.56 Å)
Structure validation

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