6WAP

Atomic-Resolution Structure of HIV-1 Capsid Tubes by Magic Angle Spinning NMR

6WAP の概要

• エントリーDOI: 10.2210/pdb6wap/pdb
• NMR情報: BMRB: 30741
• 分子名称: HIV-1 capsid protein (1 entity in total)
• 機能のキーワード: magic angle spinning nmr, hiv-1 capsid, ca protein assemblies, hiv-aids, viral protein
• 由来する生物種: Human immunodeficiency virus 1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25630.43

構造登録者

Lu, M.,Russell, R.W.,Bryer, A.,Quinn, C.M.,Hou, G.,Zhang, H.,Schwieters, C.D.,Perilla, J.R.,Gronenborn, A.M.,Polenova, T. (登録日: 2020-03-25, 公開日: 2020-09-02, 最終更新日: 2024-05-15)

主引用文献

Lu, M.,Russell, R.W.,Bryer, A.J.,Quinn, C.M.,Hou, G.,Zhang, H.,Schwieters, C.D.,Perilla, J.R.,Gronenborn, A.M.,Polenova, T.
Atomic-resolution structure of HIV-1 capsid tubes by magic-angle spinning NMR.
Nat.Struct.Mol.Biol., 27:863-869, 2020

PubMed Abstract: HIV-1 capsid plays multiple key roles in viral replication, and inhibition of capsid assembly is an attractive target for therapeutic intervention. Here, we report the atomic-resolution structure of capsid protein (CA) tubes, determined by magic-angle spinning NMR and data-guided molecular dynamics simulations. Functionally important regions, including the NTD β-hairpin, the cyclophilin A-binding loop, residues in the hexamer central pore, and the NTD-CTD linker region, are well defined. The structure of individual CA chains, their arrangement in the pseudo-hexameric units of the tube and the inter-hexamer interfaces are consistent with those in intact capsids and substantially different from the organization in crystal structures, which feature flat hexamers. The inherent curvature in the CA tubes is controlled by conformational variability of residues in the linker region and of dimer and trimer interfaces. The present structure reveals atomic-level detail in capsid architecture and provides important guidance for the design of novel capsid inhibitors.

PubMed: 32901160
DOI: 10.1038/s41594-020-0489-2

実験手法

SOLID-STATE NMR