Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function.

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 mutagenes

SUBMITTER: Byeon IJ 

PROVIDER: S-EPMC2782912 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature