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(1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a
Nonstructural protein (nsp) 3 is the largest of 16 nsps translated from the murine hepatitis virus (MHV) genome. The N-terminal most domain of nsp3, nsp3a, has been identified by reverse genetics as a likely binding partner of MHV nucleocapsid protein. Here we report the backbone and side chain reso...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587040/ https://www.ncbi.nlm.nih.gov/pubmed/23135776 http://dx.doi.org/10.1007/s12104-012-9443-5 |
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author | Keane, Sarah C. Giedroc, David P. |
author_facet | Keane, Sarah C. Giedroc, David P. |
author_sort | Keane, Sarah C. |
collection | PubMed |
description | Nonstructural protein (nsp) 3 is the largest of 16 nsps translated from the murine hepatitis virus (MHV) genome. The N-terminal most domain of nsp3, nsp3a, has been identified by reverse genetics as a likely binding partner of MHV nucleocapsid protein. Here we report the backbone and side chain resonance assignments of MHV nsp3a (residues 1-114). |
format | Online Article Text |
id | pubmed-3587040 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-35870402015-04-01 (1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a Keane, Sarah C. Giedroc, David P. Biomol NMR Assign Article Nonstructural protein (nsp) 3 is the largest of 16 nsps translated from the murine hepatitis virus (MHV) genome. The N-terminal most domain of nsp3, nsp3a, has been identified by reverse genetics as a likely binding partner of MHV nucleocapsid protein. Here we report the backbone and side chain resonance assignments of MHV nsp3a (residues 1-114). Springer Netherlands 2012-11-08 2014 /pmc/articles/PMC3587040/ /pubmed/23135776 http://dx.doi.org/10.1007/s12104-012-9443-5 Text en © Springer Science+Business Media Dordrecht 2012 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 Keane, Sarah C. Giedroc, David P. (1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a |
title | (1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a |
title_full | (1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a |
title_fullStr | (1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a |
title_full_unstemmed | (1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a |
title_short | (1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a |
title_sort | (1)h, (13)c, (15)n resonance assignments of murine hepatitis virus nonstructural protein 3a |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587040/ https://www.ncbi.nlm.nih.gov/pubmed/23135776 http://dx.doi.org/10.1007/s12104-012-9443-5 |
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