1H, 13C and 15N backbone and partial side-chain resonance assignments of the C-terminal domain of HIV-1 Pr55Gag encompassed in NCp15

During HIV-1 assembly, the Pr55 Gag polyprotein precursor (Gag) interacts with the genomic RNA, with lipids of the plasma membrane, with host proteins (ALIX, TSG101) through the ESCRT complex, with the viral protein Vpr and are involved in intermolecular interactions with other Pr55 Gag proteins. Th...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2018-04, Vol.12 (1), p.139-143
Main Authors: Larue, Valéry, Catala, Marjorie, Belfetmi, Anissa, Zargarian, Loussiné, Mauffret, Olivier, Tisné, Carine
Format: Article
Language:English
Subjects:
Biochemistry
Biochemistry, Molecular Biology
Biological and Medical Physics
Biophysics
Life Sciences
Physics
Physics and Astronomy
Polymer Sciences
Structural Biology
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Summary:During HIV-1 assembly, the Pr55 Gag polyprotein precursor (Gag) interacts with the genomic RNA, with lipids of the plasma membrane, with host proteins (ALIX, TSG101) through the ESCRT complex, with the viral protein Vpr and are involved in intermolecular interactions with other Pr55 Gag proteins. This network of interactions is responsible for the formation of the viral particle, the selection of genomic RNA and the packaging of Vpr. The C-terminal domain of Gag encompassed in NCp15 is involved in the majority of these interactions, either by its nucleocapsid or its p6 domains. We study the NCp15 protein as a model of the C-terminal domain of Gag to better understand the role of this domain in the assembly and budding of HIV-1. Here, we report the 1 H, 13 C and 15 N chemical shift assignments of NCp15 obtained by heteronuclear multidimensional NMR spectroscopy as well as the analysis of its secondary structure in solution. These assignments of NCp15 pave the way for interaction studies with its numerous partners.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-017-9796-x