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Localizing Conformational Hinges by NMR: Where Do Hepatitis B Virus Core Proteins Adapt for Capsid Assembly?
Author(s) -
Lecoq Lauriane,
Wang Shishan,
Wiegand Thomas,
Bressanelli Stéphane,
Nassal Michael,
Meier Beat H.,
Böckmann Anja
Publication year - 2018
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201800211
Subject(s) - dihedral angle , icosahedral symmetry , capsid , chemistry , crystallography , hinge , protein structure , nuclear magnetic resonance spectroscopy , molecule , stereochemistry , hydrogen bond , biochemistry , physics , organic chemistry , classical mechanics , gene
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 although, 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.