4MWF

Structure of Hepatitis C Virus Envelope Glycoprotein E2 core bound to broadly neutralizing antibody AR3C

Summary for 4MWF

• Entry DOI: 10.2210/pdb4mwf/pdb
• Descriptor: Fab AR3C heavy chain, Fab AR3C light chain, Envelope glycoprotein E2, ... (6 entities in total)
• Functional Keywords: immunoglobulin fold, hcv e2, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 146155.95

Authors

Kong, L.,Wilson, I.A.,Law, M. (deposition date: 2013-09-24, release date: 2013-12-11, Last modification date: 2024-11-06)

Primary citation

Kong, L.,Giang, E.,Nieusma, T.,Kadam, R.U.,Cogburn, K.E.,Hua, Y.,Dai, X.,Stanfield, R.L.,Burton, D.R.,Ward, A.B.,Wilson, I.A.,Law, M.
Hepatitis C virus e2 envelope glycoprotein core structure.
Science, 342:1090-1094, 2013

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 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.

PubMed: 24288331
DOI: 10.1126/science.1243876

Experimental method

X-RAY DIFFRACTION (2.645 Å)