5L1Z

TAR complex with HIV-1 Tat-AFF4-P-TEFb

5L1Z の概要

• エントリーDOI: 10.2210/pdb5l1z/pdb
• 関連するPDBエントリー: 4OGR
• 分子名称: Cyclin-dependent kinase 9, Cyclin-T1, AF4/FMR2 family member 4, ... (6 entities in total)
• 機能のキーワード: hiv-1 tar, protein-rna complex, transcription, protein kinase, transcription-rna complex, transcription/rna
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 87052.07

構造登録者

Schulze-Gahmen, U.,Hurley, J. (登録日: 2016-07-29, 公開日: 2016-10-26, 最終更新日: 2024-10-30)

主引用文献

Schulze-Gahmen, U.,Echeverria, I.,Stjepanovic, G.,Bai, Y.,Lu, H.,Schneidman-Duhovny, D.,Doudna, J.A.,Zhou, Q.,Sali, A.,Hurley, J.H.
Insights into HIV-1 proviral transcription from integrative structure and dynamics of the Tat:AFF4:P-TEFb:TAR complex.
Elife, 5:-, 2016

PubMed Abstract: HIV-1 Tat hijacks the human superelongation complex (SEC) to promote proviral transcription. Here we report the 5.9 Å structure of HIV-1 TAR in complex with HIV-1 Tat and human AFF4, CDK9, and CycT1. The TAR central loop contacts the CycT1 Tat-TAR recognition motif (TRM) and the second Tat Zn-binding loop. Hydrogen-deuterium exchange (HDX) shows that AFF4 helix 2 is stabilized in the TAR complex despite not touching the RNA, explaining how it enhances TAR binding to the SEC 50-fold. RNA SHAPE and SAXS data were used to help model the extended (Tat Arginine-Rich Motif) ARM, which enters the TAR major groove between the bulge and the central loop. The structure and functional assays collectively support an integrative structure and a bipartite binding model, wherein the TAR central loop engages the CycT1 TRM and compact core of Tat, while the TAR major groove interacts with the extended Tat ARM.

PubMed: 27731797
DOI: 10.7554/eLife.15910

実験手法

X-RAY DIFFRACTION (5.9 Å)