1esx

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: turn]]
[[Category: turn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:44:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:10 2008''

Revision as of 10:31, 21 February 2008

Image:1esx.jpg

1esx

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1H, 15N AND 13C STRUCTURE OF THE HIV-1 REGULATORY PROTEIN VPR : COMPARISON WITH THE N-AND C-TERMINAL DOMAIN STRUCTURE, (1-51)VPR AND (52-96)VPR

Overview

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.

About this Structure

1ESX is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

NMR 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., Wecker K, Morellet N, Bouaziz S, Roques BP, Eur J Biochem. 2002 Aug;269(15):3779-88. PMID:12153575

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