VprBP

From Proteopedia

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Revision as of 08:27, 19 December 2017

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function VPRBP (VPR-binding protein) is a HIV-1 WD40 protein is essential for DNA replication and embryonic development[1]. VPRBP has intrinsic kinase activity and is capable of phosphorylating histone H2A. Recruitment of VPRBP by VPR is essential for HIV-1 VPR activity of initiating the host cell response cycle arresting its G(2) phase following mitosis[2]. Disease Relevance VPRBP inhibition could be a strategy for the development of anticancer therapeutics[3]. Structural highlights

3D Structures of VPRBP

Updated on 19-December-2017

4pxw – hVPRBP residues 1039-1401 (mutant) - human
3wa0 – hVPRBP residues 1417-1506 + merlin
4p7i – hVPRBP residues 998-1058 + merlin
4z8l, 5aja, 4cc9 – hVPRBP residues 1057-1396 + VPX + SAMHD1
5jk7 – hVPRBP residues 1045-1396 + VPR + DNA damage-binding protein + uracil-DNA glycosylase

References

1. ↑ McCall CM, Miliani de Marval PL, Chastain PD 2nd, Jackson SC, He YJ, Kotake Y, Cook JG, Xiong Y. Human immunodeficiency virus type 1 Vpr-binding protein VprBP, a WD40 protein associated with the DDB1-CUL4 E3 ubiquitin ligase, is essential for DNA replication and embryonic development. Mol Cell Biol. 2008 Sep;28(18):5621-33. doi: 10.1128/MCB.00232-08. Epub 2008 Jul , 7. PMID:18606781 doi:http://dx.doi.org/10.1128/MCB.00232-08
2. ↑ Le Rouzic E, Belaidouni N, Estrabaud E, Morel M, Rain JC, Transy C, Margottin-Goguet F. HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase. Cell Cycle. 2007 Jan 15;6(2):182-8. Epub 2007 Jan 17. PMID:17314515
3. ↑ Kim K, Kim JM, Kim JS, Choi J, Lee YS, Neamati N, Song JS, Heo K, An W. VprBP has intrinsic kinase activity targeting histone H2A and represses gene transcription. Mol Cell. 2013 Nov 7;52(3):459-67. doi: 10.1016/j.molcel.2013.09.017. Epub 2013, Oct 17. PMID:24140421 doi:http://dx.doi.org/10.1016/j.molcel.2013.09.017