Structural consequences of phosphorylation of two serine residues in the cytoplasmic domain of HIV-1 VpU

Journal of Peptide Science : an Official Publication of the European Peptide Society
Marc WittlichDieter Willbold

Abstract

The human immunodeficiency virus type 1 (HIV-1) protein U (VpU) is an accessory protein responsible for enhancement of viral particle release and down regulation of the T-lymphocyte coreceptor CD4. Direct binding between the cytoplasmic domains of CD4 and VpU as well as phosphorylation of serines 53 and 57 in the cytoplasmic domain of VpU plays a central role in CD4 downregulation. We investigated structural consequences of phosphorylation of the two serines using nuclear magnetic resonance spectroscopy. A uniformly 15N and 13C stable isotope-labeled 45-residue peptide comprising the cytoplasmic domain of VpU (VpUcyt) was recombinantly produced in E .coli. The peptide forms two helices (commonly referred to as helix 2 and 3) in the presence of membrane mimicking dodecylphosphocholine (DPC) micelles, which flank a flexible region containing the two phosphorylation sites. Phosphorylation does not cause any drastic structural changes in the secondary structure of VpUcyt. However, an N-terminal elongation of helix 3 and a slightly reduced helicity at the C-terminus of helix 2 are observed upon phosphorylation based on characteristic changes of 13Calpha and 13Cbeta chemical shifts. Phosphorylation also reduces the local mobility of ...Continue Reading

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Citations

Sep 23, 2010·Molecular Aspects of Medicine·Amy Andrew, Klaus Strebel
Sep 13, 2015·Biochimica Et Biophysica Acta·Hua ZhangStanley J Opella
Jun 10, 2015·Current Opinion in Virology·Stanley J Opella
Jan 26, 2016·Biochimica Et Biophysica Acta·Wolfgang B FischerDieter Heermann
Aug 29, 2021·Viruses·Nabab Khan, Jonathan D Geiger

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