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6VLK

A varicella-zoster virus glycoprotein

6VLK の概要
エントリーDOI10.2210/pdb6vlk/pdb
分子名称Envelope glycoprotein B, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
機能のキーワードviral membrane glycoprotein, viral protein
由来する生物種Varicella-zoster virus (strain Oka vaccine) (HHV-3)
タンパク質・核酸の鎖数2
化学式量合計173078.84
構造登録者
Xing, Y. (登録日: 2020-01-24, 公開日: 2020-07-15, 最終更新日: 2024-10-16)
主引用文献Oliver, S.L.,Xing, Y.,Chen, D.H.,Roh, S.H.,Pintilie, G.D.,Bushnell, D.A.,Sommer, M.H.,Yang, E.,Carfi, A.,Chiu, W.,Arvin, A.M.
A glycoprotein B-neutralizing antibody structure at 2.8 angstrom uncovers a critical domain for herpesvirus fusion initiation.
Nat Commun, 11:4141-4141, 2020
Cited by
PubMed Abstract: Members of the Herpesviridae, including the medically important alphaherpesvirus varicella-zoster virus (VZV), induce fusion of the virion envelope with cell membranes during entry, and between cells to form polykaryocytes in infected tissues. The conserved glycoproteins, gB, gH and gL, are the core functional proteins of the herpesvirus fusion complex. gB serves as the primary fusogen via its fusion loops, but functions for the remaining gB domains remain unexplained. As a pathway for biological discovery of domain function, our approach used structure-based analysis of the viral fusogen together with a neutralizing antibody. We report here a 2.8 Å cryogenic-electron microscopy structure of native gB recovered from VZV-infected cells, in complex with a human monoclonal antibody, 93k. This high-resolution structure guided targeted mutagenesis at the gB-93k interface, providing compelling evidence that a domain spatially distant from the gB fusion loops is critical for herpesvirus fusion, revealing a potential new target for antiviral therapies.
PubMed: 32811830
DOI: 10.1038/s41467-020-17911-0
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4529 Å)
構造検証レポート
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件を2024-11-13に公開中

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