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PDBsum entry 2kod
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Viral protein
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PDB id
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2kod
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References listed in PDB file
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Key reference
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Title
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Structural convergence between cryo-Em and nmr reveals intersubunit interactions critical for HIV-1 capsid function.
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Authors
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I.J.Byeon,
X.Meng,
J.Jung,
G.Zhao,
R.Yang,
J.Ahn,
J.Shi,
J.Concel,
C.Aiken,
P.Zhang,
A.M.Gronenborn.
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Ref.
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Cell, 2009,
139,
780-790.
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PubMed id
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Abstract
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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.
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