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A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly
Bacteriophage P22, a double-stranded DNA (dsDNA) virus, has a nonconserved 124-amino-acid accessory domain inserted into its coat protein, which has the canonical HK97 protein fold. This I domain is involved in virus capsid size determination and stability, as well as protein folding. The nuclear ma...
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| Published in: | J Virol |
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| Main Authors: | , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
American Society for Microbiology
2015
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4580156/ https://ncbi.nlm.nih.gov/pubmed/26269173 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.01629-15 |
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