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Basic Characteristics of Mutations
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Mutation Site
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S208T |
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Mutation Site Sentence
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We tested other amino acids in position 208 and found that S208D had effects similar to but slightly less pronounced than those of S208E (Fig. (Fig.3)3) and that the protein with the conservative mutation S208T differed little from the wild type. |
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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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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
|
|
PMID
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19144704
|
|
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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