Localizing conformational hinges by NMR: where do HBV core proteins adapt for capsid assembly?
 

Localizing conformational hinges by NMR: where do HBV core proteins adapt for capsid assembly?

Localizing conformational hinges by NMR: where do HBV core proteins adapt for capsid assembly?

Chemphyschem. 2018 Mar 15;:

Authors: Lecoq L, Wang S, Wiegand T, Bressanelli S, Nassal M, Meier BH, Böckmann A

Abstract
The hepatitis B virus (HBV) icosahedral nucleocapsid is assembled from 240 chemically identical core protein molecules and, structurally, comprises four groups of symmetrically nonequivalent subunits. We show here that this asymmetry is reflected in solid-state NMR spectra of the capsids in which peak splitting is observed for a subset of residues. We compare this information to dihedral angle variations from available 3D structures, and also to computational predictions of dynamic domains and molecular hinges. We find that while, at the given resolution, dihedral angles variations directly obtained from the X-ray structures are not precise enough to be interpreted, the chemical-shift information from NMR correlates, and interestingly goes beyond, information from bioinformatics approaches. Our study reveals the high sensitivity with which NMR can detect the residues allowing the subtle conformational adaptations needed in lattice formation. Our findings are important for understanding the formation and modulation of protein assemblies in general.


PMID: 29542854 [PubMed - as supplied by publisher]



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