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Basic Characteristics of Mutations
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Mutation Site
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R213A |
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Mutation Site Sentence
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Indeed, D236 as well as S208, S209, D212, and R213 within SSENDRL is partly solvent exposed and may conceivably interact with a replication factor that recognizes the hairpin structure of BZLF1. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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BZLF1 |
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Standardized Encoding Gene
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BZLF1
|
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Genotype/Subtype
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- |
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Viral Reference
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-
|
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Functional Impact and Mechanisms
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Disease
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-
|
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Immune
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- |
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Target Gene
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-
|
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
|
- |
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Location
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- |
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Literature Information
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PMID
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19144704
|
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Title
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Interaction of Epstein-Barr virus BZLF1 C-terminal tail structure and core zipper is required for DNA replication but not for promoter transactivation
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Author
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McDonald CM,Petosa C,Farrell PJ
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Journal
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Journal of virology
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Journal Info
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2009 Apr;83(7):3397-401
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Abstract
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The Epstein-Barr virus (EBV) protein BZLF1 contains a bZIP DNA binding domain in which C-terminal tail residues fold back against a zipper region that forms a coiled coil and mediates dimerization. Point mutagenesis in the zipper region reveals the importance of individual residues within the (208)SSENDRLR(215) sequence that is conserved in C/EBP for transactivation and EBV DNA replication. The restoration of BZLF1 DNA replication activity by the complementation of two deleterious mutations (S208E and D236K) indicates that the interaction of the C-terminal tail and the core zipper is required for DNA replication, identifying a functional role for this structural feature unique to BZLF1.
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Sequence Data
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-
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