4MWF

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

4MWF の概要

• エントリーDOI: 10.2210/pdb4mwf/pdb
• 分子名称: Fab AR3C heavy chain, Fab AR3C light chain, Envelope glycoprotein E2, ... (6 entities in total)
• 機能のキーワード: immunoglobulin fold, hcv e2, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 146155.95

構造登録者

Kong, L.,Wilson, I.A.,Law, M. (登録日: 2013-09-24, 公開日: 2013-12-11, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.645 Å)