Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase

In this paper, we report the variations of amino acid residues between H5N1 and H1N1 swine flu neuraminidase sequences at protein level. Random search in NCBI Flu database resulted in Canadian viral gene and analysis using blast technique revealed sites that are variant among sequences for which 3-d...

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Autores principales: Nageswara Rao, G., Srinivasarao, P., Apparao, A., Rama Krishna Rao, T. K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7124146/
http://dx.doi.org/10.1007/978-81-322-0740-5_68
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author Nageswara Rao, G.
Srinivasarao, P.
Apparao, A.
Rama Krishna Rao, T. K.
author_facet Nageswara Rao, G.
Srinivasarao, P.
Apparao, A.
Rama Krishna Rao, T. K.
author_sort Nageswara Rao, G.
collection PubMed
description In this paper, we report the variations of amino acid residues between H5N1 and H1N1 swine flu neuraminidase sequences at protein level. Random search in NCBI Flu database resulted in Canadian viral gene and analysis using blast technique revealed sites that are variant among sequences for which 3-dimensional structures were known. PDB summary database and multiple alignments were employed for validation of the results. Based on the mutations observed within active site region, homology derived model was constructed using swiss-pdb viewer. The residue variation observed was with respect to Tyr347 in H5N1 versus Asn344 in H1N1 neuraminidase sequence, which resulted in geometrical modification of ligand binding domain.
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spelling pubmed-71241462020-04-06 Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase Nageswara Rao, G. Srinivasarao, P. Apparao, A. Rama Krishna Rao, T. K. Proceedings of International Conference on Advances in Computing Article In this paper, we report the variations of amino acid residues between H5N1 and H1N1 swine flu neuraminidase sequences at protein level. Random search in NCBI Flu database resulted in Canadian viral gene and analysis using blast technique revealed sites that are variant among sequences for which 3-dimensional structures were known. PDB summary database and multiple alignments were employed for validation of the results. Based on the mutations observed within active site region, homology derived model was constructed using swiss-pdb viewer. The residue variation observed was with respect to Tyr347 in H5N1 versus Asn344 in H1N1 neuraminidase sequence, which resulted in geometrical modification of ligand binding domain. 2012 /pmc/articles/PMC7124146/ http://dx.doi.org/10.1007/978-81-322-0740-5_68 Text en © Springer India 2013 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Nageswara Rao, G.
Srinivasarao, P.
Apparao, A.
Rama Krishna Rao, T. K.
Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase
title Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase
title_full Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase
title_fullStr Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase
title_full_unstemmed Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase
title_short Variation in Active Site Amino Residues of H1N1 Swine Flu Neuraminidase
title_sort variation in active site amino residues of h1n1 swine flu neuraminidase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7124146/
http://dx.doi.org/10.1007/978-81-322-0740-5_68
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