Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution. NLM AIDSLINE Important note: Information in this article was accurate in 1997. The state of the art may have changed since the publication date.

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Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution.

Eur J Biochem. 1997 May 1;245(3):581-8. Unique Identifier : AIDSLINE MED/97325981
Willbold D; Hoffmann S; Rosch P; Lehrstuhl fur Biopolymere, Universitat Bayreuth, Germany.; Dieter.Willbold@uni-bayreuth.de

Abstract: The human immunodeficiency virus type 1 Vpu protein enhances virus particle release from infected cells, decreases the tendency of syncytia formation and induces degradation of human CD4 receptor. It is known that the cytoplasmic part of Vpu is responsible for direct interaction to and degradation of CD4. The tertiary fold of the Vpu cytoplasmic domain in aqueous solution was determined employing NMR spectroscopy and molecular-dynamics simulated-annealing protocols. We found a very well defined amphipathic alpha-helix in the membrane proximal part (40-50), a less well defined helix (60-68), and a short alpha-helix at the C-terminus (75-79). We further determined the overall tertiary structure based on long-range nuclear Overhauser enhancement effects. Correlation of results from mutation experiments of Vpu and the structure data is discussed.
Keywords: *Gene Products, vpu/CHEMISTRY *HIV-1 *Protein Folding *Protein Structure, Secondary *Protein Structure, TertiaryKWDgeneproducts,vpu/chemistryKWDhiv-1KWDproteinfoldingKWDproteinstructure,secondaryKWDproteinstructure,tertiary
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Copyright © 1997 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

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