View source for VprBP

<StructureSection load='5jk7' size='350' side='right' caption='Human VprBP residues 1045-1396 (pink) complex with Vpr (cyan), DNA damage-binding protein (green) and uracil-DNA glycosylase (yellow) (PDB code [[5jk7]])' scene='77/776391/Cv/2'>

== Function ==

'''VprBP''' ('''VPR-binding protein''') or '''DDB1- and CUL4-associated factor 1''' or '''DCAF1''' is a HIV-1 WD40 protein is essential for DNA replication and embryonic development<ref>PMID:18606781</ref>.  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<ref>PMID:17314515</ref>.  VprBP interacts with merlin which is then recruited to the E3 ligase complex resulting in its polyubiquitination and consequently its proteasome-mediated degradation<ref>PMID:18332868</ref>.

== Relevance ==

VprBP inhibition could be a strategy for the development of anticancer therapeutics<ref>PMID:24140421</ref>.

== Structural highlights ==

The interactions between VprBP and Vpr are located in a cleft formed by <scene name='77/776391/Cv/10'>VprBD canonical WD40 seven-blade β-propeller</scene> ({{Template:ColorKey_Helix}}, {{Template:ColorKey_Strand}}, {{Template:ColorKey_Loop}}, {{Template:ColorKey_Turn}}) which is <scene name='77/776391/Cv/11'>lined by acidic residues on one end and hydrophobic residues at the center</scene> ({{Template:ColorKey_Charge_Anionic}} / {{Template:ColorKey_Charge_Cationic}}; {{Template:ColorKey_Hydrophobic}},  {{Template:ColorKey_Polar}}). The interactions are formed by <scene name='77/776391/Cv/12'>hydrogen bonds</scene>, <scene name='77/776391/Cv/13'>Vpr Phe residue buried in VprBP hydrophobic pocket</scene> and <scene name='77/776391/Cv/14'>VprBP Trp binding to residues in Vpr pocket</scene><ref>PMID:27571178</ref>.

== 3D Structures of VprBP ==
[[VprBP 3D structures]]

== References ==
<references/>
</StructureSection>
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