6WAP
Atomic-Resolution Structure of HIV-1 Capsid Tubes by Magic Angle Spinning NMR
Summary for 6WAP
| Entry DOI | 10.2210/pdb6wap/pdb |
| NMR Information | BMRB: 30741 |
| Descriptor | HIV-1 capsid protein (1 entity in total) |
| Functional Keywords | magic angle spinning nmr, hiv-1 capsid, ca protein assemblies, hiv-aids, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 25630.43 |
| Authors | 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. (deposition date: 2020-03-25, release date: 2020-09-02, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 32901160DOI: 10.1038/s41594-020-0489-2 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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