Related ArticlesNMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains.
Eur J Biochem. 2002 Aug;269(15):3779-88
Authors: Wecker K, Morellet N, Bouaziz S, Roques BP
The human immunodeficiency virus type 1, HIV-1, genome encodes a highly conserved regulatory gene product, Vpr (96 amino acids), which is incorporated into virions in quantities equivalent to those of the viral Gag protein. In infected cells, Vpr is believed to function during the early stages of HIV-1 replication (such as transcription of the proviral genome and migration of preintegration nuclear complex), blocks cells in G2 phase and triggers apoptosis. Vpr also plays a critical role in long-term AIDS disease by inducing viral infection in nondividing cells such as monocytes and macrophages. To gain deeper insight of the structure-function relationship of Vpr, the intact protein (residues 1-96) was synthesized. Its three-dimensional structure was analysed using circular dichroism and two-dimensional 1H- and 15N-NMR and refined by restrained molecular dynamics. In addition, 15N relaxation parameters (T1, T2) and heteronuclear 1H-15N NOEs were measured. The structure of the protein is characterized by a well-defined gamma turn(14-16)-alpha helix(17-33)-turn(34-36), followed by a alpha helix(40-48)-loop(49-54)-alpha helix(55-83) domain and ends with a very flexible C-terminal sequence. This structural determination of the whole intact Vpr molecule provide insights into the biological role played by this protein during the virus life cycle, as such amphipathic helices are believed to be involved in protein-lipid bilayers, protein-protein and/or protein-nucleic acid interactions.
[NMR paper] NMR structure of the HIV-1 regulatory protein VPR.
NMR structure of the HIV-1 regulatory protein VPR.
Related Articles NMR structure of the HIV-1 regulatory protein VPR.
J Mol Biol. 2003 Mar 14;327(1):215-27
Authors: Morellet N, Bouaziz S, Petitjean P, Roques BP
The human immunodeficiency virus type 1 (HIV-1) genome encodes a highly conserved regulatory gene product, Vpr (96 residues, 14kDa), which is incorporated into virions. In the infected cells, Vpr, expressed late in the virus cycle, is believed to function in the early phases of HIV-1 replication, such as nuclear migration of...
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[NMR paper] NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
Related Articles NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr.
Eur J Biochem. 1999 Dec;266(2):359-69
Authors: Wecker K, Roques BP
The human immunodeficiency virus type 1 (HIV-1) genome encodes a highly conserved 16 kDa regulatory gene product, Vpr (viral protein of regulation, 96 amino acid residues), which is incorporated into virions, in quantities equivalent to those of the viral Gag proteins. In the infected cells, Vpr is...
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Solution NMR structure of the plasmid-encoded fimbriae regulatory protein PefI from S
Solution NMR structure of the plasmid-encoded fimbriae regulatory protein PefI from Salmonella enterica serovar Typhimurium.
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Proteins. 2010 Sep 13;
Authors: Aramini JM, Rossi P, Cort JR, Ma LC, Xiao R, Acton TB, Montelione GT
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NMR structure of the protein NP_247299.1: comparison with the crystal structure.
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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1367-80
Authors: Jaudzems K, Geralt M, Serrano P, Mohanty B, Horst R, Pedrini B, Elsliger MA, Wilson IA, Wüthrich K
The NMR structure of the protein NP_247299.1 in solution at 313 K has been determined and is compared with the X-ray crystal structure, which was also solved in the Joint Center for...
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[NMR paper] Probing protein structure by solvent perturbation of NMR spectra. A comparison with p
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra. A comparison with photochemically induced dynamic nuclear polarization techniques applied to native alpha-lactalbumin.
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[NMR paper] Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
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Biochemistry. 1992 Sep 22;31(37):8790-8
Authors: Sönnichsen FD, Van Eyk JE, Hodges RS, Sykes BD
The structure of a synthetic peptide comprising the 28 amino-terminal residues of actin has been examined by 1H-NMR and CD spectroscopy. The peptide is largely unstructured and flexible in solution but becomes...
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[NMR paper] Exploring the dynamic information content of a protein NMR structure: comparison of a
Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
Proteins. 1999 Jul 1;36(1):87-110
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[NMR paper] NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: m
NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions.
J Mol Biol. 1999 Feb 5;285(5):2105-17
Authors: Schüler W, Wecker K, de Rocquigny H, Baudat Y, Sire J, Roques BP
The HIV-1 regulatory protein Vpr (96 amino...
NMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol. Comparison
Linear Mode
