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-Structure paper
Title | Hepatitis C virus E2 envelope glycoprotein core structure. |
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Journal, issue, pages | Science, Vol. 342, Issue 6162, Page 1090-1094, Year 2013 |
Publish date | Nov 29, 2013 |
Authors | Leopold Kong / Erick Giang / Travis Nieusma / Rameshwar U Kadam / Kristin E Cogburn / Yuanzi Hua / Xiaoping Dai / Robyn L Stanfield / Dennis R Burton / Andrew B Ward / Ian A Wilson / Mansun Law / |
PubMed Abstract | Hepatitis C virus (HCV), a Hepacivirus, is a major cause of viral hepatitis, liver cirrhosis, and hepatocellular carcinoma. HCV envelope glycoproteins E1 and E2 mediate fusion and entry into host ...Hepatitis C virus (HCV), a Hepacivirus, is a major cause of viral hepatitis, liver cirrhosis, and hepatocellular carcinoma. HCV envelope glycoproteins E1 and E2 mediate fusion and entry into host cells and are the primary targets of the humoral immune response. The crystal structure of the E2 core bound to broadly neutralizing antibody AR3C at 2.65 angstroms reveals a compact architecture composed of a central immunoglobulin-fold β sandwich flanked by two additional protein layers. The CD81 receptor binding site was identified by electron microscopy and site-directed mutagenesis and overlaps with the AR3C epitope. The x-ray and electron microscopy E2 structures differ markedly from predictions of an extended, three-domain, class II fusion protein fold and therefore provide valuable information for HCV drug and vaccine design. |
External links | Science / PubMed:24288331 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.645 - 20.0 Å |
Structure data | EMDB-5759: EMDB-5760: EMDB-5761: PDB-4mwf: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | IMMUNE SYSTEM / Immunoglobulin Fold / HCV E2 |