5L1Z
TAR complex with HIV-1 Tat-AFF4-P-TEFb
Summary for 5L1Z
| Entry DOI | 10.2210/pdb5l1z/pdb |
| Related | 4OGR |
| Descriptor | Cyclin-dependent kinase 9, Cyclin-T1, AF4/FMR2 family member 4, ... (6 entities in total) |
| Functional Keywords | hiv-1 tar, protein-rna complex, transcription, protein kinase, transcription-rna complex, transcription/rna |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 87052.07 |
| Authors | Schulze-Gahmen, U.,Hurley, J. (deposition date: 2016-07-29, release date: 2016-10-26, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 27731797DOI: 10.7554/eLife.15910 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (5.9 Å) |
Structure validation
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