VprBP: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Jaime Prilusky, Alexander Berchansky

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-<StructureSection load='5jk7' size='400' 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/1'>
+<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''') 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>.
+'''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 ==
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 == Structural highlights ==
-The interactions between VprBP and Vpr are located in a cleft formed by VprBD canonical WD40 seven-blade β-propeller which is lined by acidic residues on one end and hydrophobic residues at the center.  The interactions are formed by hydrogen bonds, Vpr Phe residue buried in VprBP hydrophobic pocket and VprBP Trp binding to residues in Vpr pocket<ref>PMID:27571178</ref>.
+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>.
-</StructureSection>
 == 3D Structures of VprBP ==
+[[VprBP 3D structures]]
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-[[4pxw]] – hVprBP residues 1039-1401 (mutant) - human <br />
-[[3wa0]] – hVprBP residues 1417-1506 + merlin  <br />
-[[4p7i]] – hVprBP residues 998-1058 + merlin  <br />
-[[4z8l]], [[5aja]], [[4cc9]] – hVprBP residues 1057-1396 + VPX + SAMHD1  <br />
-[[5jk7]] – hVprBP residues 1045-1396 + Vpr + DNA damage-binding protein + uracil-DNA glycosylase <br />
 == References ==
 <references/>
+</StructureSection>
 [[Category:Topic Page]]