Article Abstract:
The Epstein-Barr virus produces an antigen that binds with the host DNA and initiates replication of the viral genome. This origin binding protein possesses a flanking domain with helical and chain structures that are directly involved in unwinding the DNA chain. DNA is unwound when the binding protein winds its own helix to tighten the DNA helix and cause the base pairings to lose their stability. Meanwhile, a core domain similar to that found in the bovine papilloma virus protein was also found that had no involvement in replication processes.
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Article Abstract:
Recognition of DNA repair proteins XPA, UNG2, and RAD52 by replication factor replication protein A (RPA) has been studied as it relates to structure. It has been found that a globular domain at the c terminus of subunit TPA32 has a specific surface that interacts in a manner like that of DNA repair enzyme UNG2 and repair factors RAD52 and XPA. Each of these acts in a different repair pathway. Results indicate a hand-off model for assembly and coordination of different components of the DNA repair machinery.
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Article Abstract:
Two independent regions, the core and the flanking DNA-binding domains, are involved in DNA binding by Epstein-Barr virus nuclear antigen 1 (EBNA1). The core DNA-binding domain of EBNA1 has a dimerization domain and a helix binding the inner portion of the EBNA1 DNA recognition element. The structure is similar to that of papillomavirus E2 protein. The n-terminal of an alpha helix in the flanking DNA binding domains abut the outer regions of the DNA recognition element.
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