5LLJ

Maedi-Visna virus (MVV) integrase C-terminal domain (residues 220-276)

5LLJ の概要

• エントリーDOI: 10.2210/pdb5llj/pdb
• 分子名称: Integrase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: integrase, visna/maedi virus, c-terminal domain, viral protein
• 由来する生物種: Maedi visna virus (strain KV1772) (MVV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13491.00

構造登録者

Pye, V.E.,Maskell, D.P.,Cherepanov, P. (登録日: 2016-07-27, 公開日: 2017-01-18, 最終更新日: 2024-01-10)

主引用文献

Ballandras-Colas, A.,Maskell, D.P.,Serrao, E.,Locke, J.,Swuec, P.,Jonsson, S.R.,Kotecha, A.,Cook, N.J.,Pye, V.E.,Taylor, I.A.,Andresdottir, V.,Engelman, A.N.,Costa, A.,Cherepanov, P.
A supramolecular assembly mediates lentiviral DNA integration.
Science, 355:93-95, 2017

PubMed Abstract: Retroviral integrase (IN) functions within the intasome nucleoprotein complex to catalyze insertion of viral DNA into cellular chromatin. Using cryo-electron microscopy, we now visualize the functional maedi-visna lentivirus intasome at 4.9 angstrom resolution. The intasome comprises a homo-hexadecamer of IN with a tetramer-of-tetramers architecture featuring eight structurally distinct types of IN protomers supporting two catalytically competent subunits. The conserved intasomal core, previously observed in simpler retroviral systems, is formed between two IN tetramers, with a pair of C-terminal domains from flanking tetramers completing the synaptic interface. Our results explain how HIV-1 IN, which self-associates into higher-order multimers, can form a functional intasome, reconcile the bulk of early HIV-1 IN biochemical and structural data, and provide a lentiviral platform for design of HIV-1 IN inhibitors.

PubMed: 28059770
DOI: 10.1126/science.aah7002

実験手法

X-RAY DIFFRACTION (1.78 Å)