Limits...
Molecular docking analysis of RN18 and VEC5 in A3G-Vif inhibition.

Sinha C, Nischal A, Pant KK, Bandaru S, Nayarisseri A, Khattri S - Bioinformation (2014)

Bottom Line: VEC 5 showed better interaction with Vif than RN18.Predicted data show that VEC5 bound Vif and RN18 bound Vif showed diminished interaction to A3G compared to inhibitor unbound Vif.However, this should be further validated using in vitro studies.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmacology and Therapeutics, King George's Medical University, (Erstwhile C.S.M. Medical University),Lucknow- 226 003, India.

ABSTRACT
The HIV-1 protein Vif is essential for in vivo viral replication that targets the human DNA-editing enzyme, APOBEC3G (A3G), which inhibits replication of retroviruses. The Vif-A3G interactions are believed to be important targets for antiviral drug development. Since the interactions of A3G and Vif evade the ubiquitination pathways in human host, the viral replication precedes which otherwise spreads infection. In this study, two potent Vif inhibitors RN 18 and VEC5 have been evaluated for their inhibitory potential employing ligand receptor and protein-protein interactions studies. VEC 5 showed better interaction with Vif than RN18. Predicted data show that VEC5 bound Vif and RN18 bound Vif showed diminished interaction to A3G compared to inhibitor unbound Vif. However, this should be further validated using in vitro studies.

No MeSH data available.


Related in: MedlinePlus

Interface residues (in ball and stick representation) between A3G (violet) and Vif (green) in A) A3G-Vif (unbound); B)A3G-Vif (bound to RN18); C) A3G-Vif (bound to VEC5)
© Copyright Policy - open-access
Related In: Results  -  Collection


getmorefigures.php?uid=PMC4248342&req=5

Figure 3: Interface residues (in ball and stick representation) between A3G (violet) and Vif (green) in A) A3G-Vif (unbound); B)A3G-Vif (bound to RN18); C) A3G-Vif (bound to VEC5)

Mentions: Three modes of protein-protein interactions were investigatedin the present study. One, interaction between inhibitorunbound Vif with A3G, Two, interaction between RN18 boundVif with A3G and three, VEC5 bound Vif and A3G interaction.Table 2 (see supplementary material) represents thecomparative binding scores of RN18 and VEC5. Vif bound toRN18 and Vif bound to VEC5 showed almost similar bindingaffinity against A3G. Evident from the scores, Vif bound toRN18 and VEC5 showed declined interaction with A3G.Figure 3A, B & C respectively shows, inhibitor unbound VifA3G interactions, RN18 bound Vif –A3G interactions andVEC5 bound Vif-A3G interactions


Molecular docking analysis of RN18 and VEC5 in A3G-Vif inhibition.

Sinha C, Nischal A, Pant KK, Bandaru S, Nayarisseri A, Khattri S - Bioinformation (2014)

Interface residues (in ball and stick representation) between A3G (violet) and Vif (green) in A) A3G-Vif (unbound); B)A3G-Vif (bound to RN18); C) A3G-Vif (bound to VEC5)
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4248342&req=5

Figure 3: Interface residues (in ball and stick representation) between A3G (violet) and Vif (green) in A) A3G-Vif (unbound); B)A3G-Vif (bound to RN18); C) A3G-Vif (bound to VEC5)
Mentions: Three modes of protein-protein interactions were investigatedin the present study. One, interaction between inhibitorunbound Vif with A3G, Two, interaction between RN18 boundVif with A3G and three, VEC5 bound Vif and A3G interaction.Table 2 (see supplementary material) represents thecomparative binding scores of RN18 and VEC5. Vif bound toRN18 and Vif bound to VEC5 showed almost similar bindingaffinity against A3G. Evident from the scores, Vif bound toRN18 and VEC5 showed declined interaction with A3G.Figure 3A, B & C respectively shows, inhibitor unbound VifA3G interactions, RN18 bound Vif –A3G interactions andVEC5 bound Vif-A3G interactions

Bottom Line: VEC 5 showed better interaction with Vif than RN18.Predicted data show that VEC5 bound Vif and RN18 bound Vif showed diminished interaction to A3G compared to inhibitor unbound Vif.However, this should be further validated using in vitro studies.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmacology and Therapeutics, King George's Medical University, (Erstwhile C.S.M. Medical University),Lucknow- 226 003, India.

ABSTRACT
The HIV-1 protein Vif is essential for in vivo viral replication that targets the human DNA-editing enzyme, APOBEC3G (A3G), which inhibits replication of retroviruses. The Vif-A3G interactions are believed to be important targets for antiviral drug development. Since the interactions of A3G and Vif evade the ubiquitination pathways in human host, the viral replication precedes which otherwise spreads infection. In this study, two potent Vif inhibitors RN 18 and VEC5 have been evaluated for their inhibitory potential employing ligand receptor and protein-protein interactions studies. VEC 5 showed better interaction with Vif than RN18. Predicted data show that VEC5 bound Vif and RN18 bound Vif showed diminished interaction to A3G compared to inhibitor unbound Vif. However, this should be further validated using in vitro studies.

No MeSH data available.


Related in: MedlinePlus