3NGB

Crystal structure of broadly and potently neutralizing antibody VRC01 in complex with HIV-1 gp120

3NGB の概要

• エントリーDOI: 10.2210/pdb3ngb/pdb
• 分子名称: Envelope glycoprotein gp160, Antigen binding fragment of heavy chain: Antibody VRC01, Antigen binding fragment of light chain: Antibody VRC01, ... (9 entities in total)
• 機能のキーワード: hiv, gp120, antibody, vrc01, neutralization, vaccine, envelope glycoprotein, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Human immunodeficiency virus 1; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 363536.47

構造登録者

Zhou, T.,Kwong, P.D. (登録日: 2010-06-11, 公開日: 2010-07-07, 最終更新日: 2024-11-27)

主引用文献

Zhou, T.,Georgiev, I.,Wu, X.,Yang, Z.Y.,Dai, K.,Finzi, A.,Do Kwon, Y.,Scheid, J.F.,Shi, W.,Xu, L.,Yang, Y.,Zhu, J.,Nussenzweig, M.C.,Sodroski, J.,Shapiro, L.,Nabel, G.J.,Mascola, J.R.,Kwong, P.D.
Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01.
Science, 329:811-817, 2010

PubMed Abstract: During HIV-1 infection, antibodies are generated against the region of the viral gp120 envelope glycoprotein that binds CD4, the primary receptor for HIV-1. Among these antibodies, VRC01 achieves broad neutralization of diverse viral strains. We determined the crystal structure of VRC01 in complex with a human immunodeficiency virus HIV-1 gp120 core. VRC01 partially mimics CD4 interaction with gp120. A shift from the CD4-defined orientation, however, focuses VRC01 onto the vulnerable site of initial CD4 attachment, allowing it to overcome the glycan and conformational masking that diminishes the neutralization potency of most CD4-binding-site antibodies. To achieve this recognition, VRC01 contacts gp120 mainly through immunoglobulin V-gene regions substantially altered from their genomic precursors. Partial receptor mimicry and extensive affinity maturation thus facilitate neutralization of HIV-1 by natural human antibodies.

PubMed: 20616231
DOI: 10.1126/science.1192819

実験手法

X-RAY DIFFRACTION (2.68 Å)