The Interaction Pattern between a Homology Model of 40S Ribosomal S9 Protein of Rhizoctonia solani and 1-Hydroxyphenaize by Docking Study

1-Hydroxyphenazine (1-OH-PHZ), a natural product from Pseudomonas aeruginosa strain SD12, was earlier reported to have potent antifungal activity against Rhizoctonia solani. In the present work, the antifungal activity of 1-OH-PHZ on 40S ribosomal S9 protein was validated by molecular docking approa...

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Autores principales: Dharni, Seema, Sanchita, Samad, Abdul, Sharma, Ashok, Patra, Dharani Dhar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4016899/
https://www.ncbi.nlm.nih.gov/pubmed/24864254
http://dx.doi.org/10.1155/2014/682946
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author Dharni, Seema
Sanchita,
Samad, Abdul
Sharma, Ashok
Patra, Dharani Dhar
author_facet Dharni, Seema
Sanchita,
Samad, Abdul
Sharma, Ashok
Patra, Dharani Dhar
author_sort Dharni, Seema
collection PubMed
description 1-Hydroxyphenazine (1-OH-PHZ), a natural product from Pseudomonas aeruginosa strain SD12, was earlier reported to have potent antifungal activity against Rhizoctonia solani. In the present work, the antifungal activity of 1-OH-PHZ on 40S ribosomal S9 protein was validated by molecular docking approach. 1-OH-PHZ showed interaction with two polar contacts with residues, Arg69 and Phe19, which inhibits the synthesis of fungal protein. Our study reveals that 1-OH-PHZ can be a potent inhibitor of 40S ribosomal S9 protein of R. solani that may be a promising approach for the management of fungal diseases.
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spelling pubmed-40168992014-05-26 The Interaction Pattern between a Homology Model of 40S Ribosomal S9 Protein of Rhizoctonia solani and 1-Hydroxyphenaize by Docking Study Dharni, Seema Sanchita, Samad, Abdul Sharma, Ashok Patra, Dharani Dhar Biomed Res Int Research Article 1-Hydroxyphenazine (1-OH-PHZ), a natural product from Pseudomonas aeruginosa strain SD12, was earlier reported to have potent antifungal activity against Rhizoctonia solani. In the present work, the antifungal activity of 1-OH-PHZ on 40S ribosomal S9 protein was validated by molecular docking approach. 1-OH-PHZ showed interaction with two polar contacts with residues, Arg69 and Phe19, which inhibits the synthesis of fungal protein. Our study reveals that 1-OH-PHZ can be a potent inhibitor of 40S ribosomal S9 protein of R. solani that may be a promising approach for the management of fungal diseases. Hindawi Publishing Corporation 2014 2014-04-22 /pmc/articles/PMC4016899/ /pubmed/24864254 http://dx.doi.org/10.1155/2014/682946 Text en Copyright © 2014 Seema Dharni et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Dharni, Seema
Sanchita,
Samad, Abdul
Sharma, Ashok
Patra, Dharani Dhar
The Interaction Pattern between a Homology Model of 40S Ribosomal S9 Protein of Rhizoctonia solani and 1-Hydroxyphenaize by Docking Study
title The Interaction Pattern between a Homology Model of 40S Ribosomal S9 Protein of Rhizoctonia solani and 1-Hydroxyphenaize by Docking Study
title_full The Interaction Pattern between a Homology Model of 40S Ribosomal S9 Protein of Rhizoctonia solani and 1-Hydroxyphenaize by Docking Study
title_fullStr The Interaction Pattern between a Homology Model of 40S Ribosomal S9 Protein of Rhizoctonia solani and 1-Hydroxyphenaize by Docking Study
title_full_unstemmed The Interaction Pattern between a Homology Model of 40S Ribosomal S9 Protein of Rhizoctonia solani and 1-Hydroxyphenaize by Docking Study
title_short The Interaction Pattern between a Homology Model of 40S Ribosomal S9 Protein of Rhizoctonia solani and 1-Hydroxyphenaize by Docking Study
title_sort interaction pattern between a homology model of 40s ribosomal s9 protein of rhizoctonia solani and 1-hydroxyphenaize by docking study
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4016899/
https://www.ncbi.nlm.nih.gov/pubmed/24864254
http://dx.doi.org/10.1155/2014/682946
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