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| For details about another HIV-1 components and its replication pathway see [[HIV and accessory proteins]]. | | For details about another HIV-1 components and its replication pathway see [[HIV and accessory proteins]]. |
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| | == Conservation == |
| | Vpr is highly conserved in HIV and simian immunodeficiency virus (SIV) {{Wikipedia|Simian_immunodeficiency_virus}}, similar retrovirus which infects non-human primates<ref>PMID:12614620</ref>. In addition, all primate lentiviruses {{Wikipedia|Lentivirus}} has vpr gene whose protein product has highly conserved motifs. HIV-2 and SIVsm lentiviruses have additionally gene - vpx. In these lentiviruses, vpr and vpx executes together the roles which HIV-1 vpr perform. Vpr and Vpx has low conservation between them. |
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Revision as of 19:35, 3 April 2018
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Function
Vpr protein (Vpr) or viral protein R is a 96 amino acid protein which encoded by the human Immunodeficiency virus type 1 (HIV-1). Vpr has several roles in the progression of acquired immunodeficiency syndrome (AIDS in Wikipedia
) disease, including regulation the HIV-1 pre-integration complex (Pre-integration_complex in Wikipedia
) nuclear import and virus replication in non-dividing macrophages[1]. Moreover, Vpr prevents mitosis of dividing infect cells by blockade at G2 phase, when the viral promoter is more active, and induced apoptosis of these cells in G1 and M phase. Both the activities of cell cycle arrest and induce apoptosis has proven to be independence by mutations that can cause only one of these affects[2].
For details about another HIV-1 components and its replication pathway see HIV and accessory proteins.
Conservation
Vpr is highly conserved in HIV and simian immunodeficiency virus (SIV) Simian_immunodeficiency_virus in Wikipedia
, similar retrovirus which infects non-human primates[3]. In addition, all primate lentiviruses Lentivirus in Wikipedia
has vpr gene whose protein product has highly conserved motifs. HIV-2 and SIVsm lentiviruses have additionally gene - vpx. In these lentiviruses, vpr and vpx executes together the roles which HIV-1 vpr perform. Vpr and Vpx has low conservation between them.
- ↑ Morellet N, Bouaziz S, Petitjean P, Roques BP. NMR structure of the HIV-1 regulatory protein VPR. J Mol Biol. 2003 Mar 14;327(1):215-27. PMID:12614620
- ↑ Gonzalez ME. The HIV-1 Vpr Protein: A Multifaceted Target for Therapeutic Intervention. Int J Mol Sci. 2017 Jan 10;18(1). pii: ijms18010126. doi: 10.3390/ijms18010126. PMID:28075409 doi:https://dx.doi.org/10.3390/ijms18010126
- ↑ Morellet N, Bouaziz S, Petitjean P, Roques BP. NMR structure of the HIV-1 regulatory protein VPR. J Mol Biol. 2003 Mar 14;327(1):215-27. PMID:12614620
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3D Structures of Vpr protein
Updated on 03-April-2018
HIV-1 – Vpr - NMR - HIV-1
HIV and accessory proteins - synthetic Vpr - NMR - HIV-1
5jk7 – Vpr + DDB1 + DCAF-1 + UNG2 – X-ray solution - HIV-1
1x9v – Dimeric structure of the Vpr C-terminal domain - NMR
1vpc - C-terminal domain of Vpr - NMR - HIV-1
1fi0 - Vpr residues 13-33 in micelles - NMR - HIV-1
1bde - NMR solution of Vpr peptides connected to cell cycle arrest and nuclear provirus transfer
5b56 - Importin subunit alpha-1 + Vpr C-terminal domain - crystallographic analysis
1kzs, 1kzt, 1kzv - Vpr residues 34-51 - NMR - HIV-1
1dsj - Vpr residues 50-75 - NMR - HIV-1
1ceu - Vpr N-terminal domain - NMR - HIV-1
1dsk - Vpr residues 59-86 - NMR - HIV-1
4u1s - HLA-I + Beta-2-microglobulin + Vpr protein - X-ray diffraction
References
proteopedia link