Vpr protein: Difference between revisions

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=== Vpr induce cell cycle arrest by recruits cellular targets for degradation<ref>PMID:27571178</ref> ===

One phenotype of Vpr expression is the induction of cell cycle arrest in G2 phase. This arrest executes by engaging of DNA damage–binding protein 1 (DDB1) and CUL4A-associated factor 1 (DCAF1) to Vpr. DCAF1 is a substrate receptor of the Cullin4–RING E3 ubiquitin ligase (CRL4) of the host ubiquitin–proteasome-mediated protein degradation pathway. Mutations in Vpr that abolish its interaction with DCAF1, or silencing of DCAF1, eliminate cell-cycle arrest. The crystal structure of DDB1–DCAF1–HIV-1–Vpr–uracil-DNA glycosylase (UNG2) complex elucidate the molecular mechanism in which Vpr inhibits DDB1 enzymatic activity and send it for degradation.

One phenotype of Vpr expression is the induction of cell cycle arrest in G2 phase. This arrest executes by engaging of DNA damage–binding protein 1 (DDB1) and CUL4A-associated factor 1 (DCAF1) to Vpr. DCAF1 is a substrate receptor of the Cullin4–RING E3 ubiquitin ligase (CRL4) of the host ubiquitin–proteasome-mediated protein degradation pathway. Mutations in Vpr that abolish its interaction with DCAF1, or silencing of DCAF1, eliminate cell-cycle arrest. The crystal structure of <scene name='75/750237/Vpr_ddb1_dcaf1_ung2/2'>DDB1–DCAF1–HIV-1–Vpr–uracil-DNA glycosylase (UNG2) complex</scene> elucidate the molecular mechanism in which Vpr inhibits DDB1 enzymatic activity and send it for degradation.

* Vpr binding to the DCAF1 WD40 by its N-terminus and α3 helix. <br/>

* Vpr uses structural mimicry to DNA to engages UNG2. <br/>

Vpr protein: Difference between revisions

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@@ Line 5: / Line 5: @@
 === Vpr induce cell cycle arrest by recruits cellular targets for degradation<ref>PMID:27571178</ref> ===
-One phenotype of Vpr expression is the induction of cell cycle arrest in G2 phase. This arrest executes by engaging of DNA damage–binding protein 1 (DDB1) and CUL4A-associated factor 1 (DCAF1) to Vpr. DCAF1 is a substrate receptor of the Cullin4–RING E3 ubiquitin ligase (CRL4) of the host ubiquitin–proteasome-mediated protein degradation pathway. Mutations in Vpr that abolish its interaction with DCAF1, or silencing of DCAF1, eliminate cell-cycle arrest. The crystal structure of DDB1–DCAF1–HIV-1–Vpr–uracil-DNA glycosylase (UNG2) complex elucidate the molecular mechanism in which Vpr inhibits DDB1 enzymatic activity and send it for degradation.
+One phenotype of Vpr expression is the induction of cell cycle arrest in G2 phase. This arrest executes by engaging of DNA damage–binding protein 1 (DDB1) and CUL4A-associated factor 1 (DCAF1) to Vpr. DCAF1 is a substrate receptor of the Cullin4–RING E3 ubiquitin ligase (CRL4) of the host ubiquitin–proteasome-mediated protein degradation pathway. Mutations in Vpr that abolish its interaction with DCAF1, or silencing of DCAF1, eliminate cell-cycle arrest. The crystal structure of <scene name='75/750237/Vpr_ddb1_dcaf1_ung2/2'>DDB1–DCAF1–HIV-1–Vpr–uracil-DNA glycosylase (UNG2) complex</scene> elucidate the molecular mechanism in which Vpr inhibits DDB1 enzymatic activity and send it for degradation.
 * Vpr binding to the DCAF1 WD40 by its N-terminus and α3 helix. <br/>
 * Vpr uses structural mimicry to DNA to engages UNG2. <br/>