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PMID:19914170

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Citation

Byeon, IJ, Meng, X, Jung, J, Zhao, G, Yang, R, Ahn, J, Shi, J, Concel, J, Aiken, C, Zhang, P and Gronenborn, AM (2009) Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139:780-90

Abstract

Mature HIV-1 particles contain conical-shaped capsids that enclose the viral RNA genome and perform essential functions in the virus life cycle. Previous structural analysis of two- and three-dimensional arrays of the capsid protein (CA) hexamer revealed three interfaces. Here, we present a cryoEM study of a tubular assembly of CA and a high-resolution NMR structure of the CA C-terminal domain (CTD) dimer. In the solution dimer structure, the monomers exhibit different relative orientations compared to previous X-ray structures. The solution structure fits well into the EM density map, suggesting that the dimer interface is retained in the assembled CA. We also identified a CTD-CTD interface at the local three-fold axis in the cryoEM map and confirmed its functional importance by mutagenesis. In the tubular assembly, CA intermolecular interfaces vary slightly, accommodating the asymmetry present in tubes. This provides the necessary plasticity to allow for controlled virus capsid dis/assembly.

Links

PubMed PMC2782912 Online version:10.1016/j.cell.2009.10.010

Keywords

Capsid Proteins/chemistry; Capsid Proteins/metabolism; Cryoelectron Microscopy; HIV-1/chemistry; HIV-1/metabolism; Nuclear Magnetic Resonance, Biomolecular; RNA, Viral/metabolism; Virus Assembly

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HV1H2:POL

enables

GO:0042802: identical protein binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HV1H2:POL

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P04585:PRO_0000042440

F

Seeded From UniProt

complete

See also

References

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