9B2H

HIV-1 wild type protease with GRL-072-17A, a substituted tetrahydrofuran derivative based on Darunavir as P2 group

これはPDB形式変換不可エントリーです。

9B2H の概要

• エントリーDOI: 10.2210/pdb9b2h/pdb
• 関連するPDBエントリー: 2IEN 3NU3
• 分子名称: Protease, SODIUM ION, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: aspartic acid protease, hiv-1 protease, darunavir, a substituted tetrahydrofuran derivative inhibitor, viral protein
• 由来する生物種: Human immunodeficiency virus 1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22504.11

構造登録者

Wang, Y.-F.,Agniswamy, J.,Ghosh, A.K.,Weber, I.T. (登録日: 2024-03-15, 公開日: 2024-07-24, 最終更新日: 2024-10-02)

主引用文献

Ghosh, A.K.,Lee, D.,Sharma, A.,Johnson, M.E.,Ghosh, A.K.,Wang, Y.F.,Agniswamy, J.,Amano, M.,Hattori, S.I.,Weber, I.T.,Mitsuya, H.
Design of substituted tetrahydrofuran derivatives for HIV-1 protease inhibitors: synthesis, biological evaluation, and X-ray structural studies.
Org.Biomol.Chem., 22:7354-7372, 2024

PubMed Abstract: Substituted tetrahydrofuran derivatives were designed and synthesized to serve as the P2 ligand for a series of potent HIV-1 protease inhibitors. Both enantiomers of the tetrahydrofuran derivatives were synthesized stereoselectivity in optically active forms using lipase-PS catalyzed enzymatic resolution as the key step. These tetrahydrofuran derivatives are designed to promote hydrogen bonding and van der Waals interactions with the backbone atoms in the S2 subsite of the HIV-1 protease active site. Several inhibitors displayed very potent HIV-1 protease inhibitory activity. A high-resolution X-ray crystal structure of an inhibitor-bound HIV-1 protease provided important insight into the ligand binding site interactions in the active site.

PubMed: 38973505
DOI: 10.1039/d4ob00506f

実験手法

X-RAY DIFFRACTION (1.32 Å)