Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus

Influenza virus causes febrile respiratory illness. The infection results in significant mortality, morbidity and economic disruption. In this bioinformatics study, we used the NS1 (the conserved nonstructural) protein of influenza A virus to demonstrate its role in infectivity. Our in silico study...

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Detalles Bibliográficos
Autores principales: Anwar, Tamanna, Khan, Asad U
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics Publishing Group 2007
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174419/
https://www.ncbi.nlm.nih.gov/pubmed/18188421
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author Anwar, Tamanna
Khan, Asad U
author_facet Anwar, Tamanna
Khan, Asad U
author_sort Anwar, Tamanna
collection PubMed
description Influenza virus causes febrile respiratory illness. The infection results in significant mortality, morbidity and economic disruption. In this bioinformatics study, we used the NS1 (the conserved nonstructural) protein of influenza A virus to demonstrate its role in infectivity. Our in silico study revealed a new Casein kinase II (CKII) phosphorylation domain at position 151-154. This domain was formed due to the mutation at position 151 (T151I). Moreover, considerable difference in the secondary structure of this protein due to mutation was also reported. It is also confirmed by contact residue analysis that the changes in secondary structure are due to mutations.
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spelling pubmed-21744192008-01-10 Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus Anwar, Tamanna Khan, Asad U Bioinformation Hypothesis Influenza virus causes febrile respiratory illness. The infection results in significant mortality, morbidity and economic disruption. In this bioinformatics study, we used the NS1 (the conserved nonstructural) protein of influenza A virus to demonstrate its role in infectivity. Our in silico study revealed a new Casein kinase II (CKII) phosphorylation domain at position 151-154. This domain was formed due to the mutation at position 151 (T151I). Moreover, considerable difference in the secondary structure of this protein due to mutation was also reported. It is also confirmed by contact residue analysis that the changes in secondary structure are due to mutations. Biomedical Informatics Publishing Group 2007-10-03 /pmc/articles/PMC2174419/ /pubmed/18188421 Text en © 2007 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Anwar, Tamanna
Khan, Asad U
Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus
title Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus
title_full Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus
title_fullStr Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus
title_full_unstemmed Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus
title_short Identification of a casein kinase II phosphorylation domain in NS1 protein of H5N1 influenza virus
title_sort identification of a casein kinase ii phosphorylation domain in ns1 protein of h5n1 influenza virus
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174419/
https://www.ncbi.nlm.nih.gov/pubmed/18188421
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AT khanasadu identificationofacaseinkinaseiiphosphorylationdomaininns1proteinofh5n1influenzavirus

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