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.
journal_name
Celljournal_title
Cellauthors
Byeon IJ,Meng X,Jung J,Zhao G,Yang R,Ahn J,Shi J,Concel J,Aiken C,Zhang P,Gronenborn AMdoi
10.1016/j.cell.2009.10.010subject
Has Abstractpub_date
2009-11-13 00:00:00pages
780-90issue
4eissn
0092-8674issn
1097-4172pii
S0092-8674(09)01298-7journal_volume
139pub_type
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