2C3A

Structure of unliganded HSV gD reveals a mechanism for receptor- mediated activation of virus entry

2C3A の概要

• エントリーDOI: 10.2210/pdb2c3a/pdb
• 関連するPDBエントリー: 1JMA 1L2G 2C36
• 分子名称: GLYCOPROTEIN D, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: virus, herpes simplex virus, hsv-1, glycoprotein d, viral protein
• 由来する生物種: HUMAN HERPESVIRUS 1 (HUMAN HERPES SIMPLEX VIRUS 1)
• 細胞内の位置: Virion membrane; Single-pass type I membrane protein (By similarity): P57083
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64778.85

構造登録者

Krummenacher, C.,Supekar, V.M.,Whitbeck, J.C.,Lazear, E.,Connolly, S.A.,Eisenberg, R.J.,Cohen, G.H.,Wiley, D.C.,Carfi, A. (登録日: 2005-10-05, 公開日: 2005-12-21, 最終更新日: 2024-10-23)

主引用文献

Krummenacher, C.,Supekar, V.M.,Whitbeck, J.C.,Lazear, E.,Connolly, S.A.,Eisenberg, R.J.,Cohen, G.H.,Wiley, D.C.,Carfi, A.
Structure of Unliganded Hsv Gd Reveals a Mechanism for Receptor-Mediated Activation of Virus Entry.
Embo J., 24:4144-, 2005

PubMed Abstract: Herpes simplex virus (HSV) entry into cells requires binding of the envelope glycoprotein D (gD) to one of several cell surface receptors. The 50 C-terminal residues of the gD ectodomain are essential for virus entry, but not for receptor binding. We have determined the structure of an unliganded gD molecule that includes these C-terminal residues. The structure reveals that the C-terminus is anchored near the N-terminal region and masks receptor-binding sites. Locking the C-terminus in the position observed in the crystals by an intramolecular disulfide bond abolished receptor binding and virus entry, demonstrating that this region of gD moves upon receptor binding. Similarly, a point mutant that would destabilize the C-terminus structure was nonfunctional for entry, despite increased affinity for receptors. We propose that a controlled displacement of the gD C-terminus upon receptor binding is an essential feature of HSV entry, ensuring the timely activation of membrane fusion.

PubMed: 16292345
DOI: 10.1038/SJ.EMBOJ.7600875

実験手法

X-RAY DIFFRACTION (2.5 Å)