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of outstanding interest. The authors determined the co-crystal structure of the EBNA1 DNA binding and dimerization domains bound to DNA. The structure reveals a new mechanism for DNA binding that has mechanistic implications for origin activation.
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of outstanding interest Bochkarev A, Barwell J, Pfuetzner R, Bochkareva E, Frappier L, Edwards AM. Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin binding protein, EBNA1, bound to DNA. Cell. 84:1996;791-800 The authors determined the co-crystal structure of the EBNA1 DNA binding and dimerization domains bound to DNA. The structure reveals a new mechanism for DNA binding that has mechanistic implications for origin activation.
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Bochkarev, A.1
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Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding protein bound to its DNA target
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of special interest. This paper describes the solution structure of the DNA binding and dimerization domain of the E2 protein from human papillomavirus as determined by NMR spectroscopy. The structure was very similar to that of the co-crystal structure of the E2 protein from bovine papillomavirus [10] but slight differences in the demerization interface were observed.
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of special interest Liang H, Petros AM, Meadows RP, Yoon HS, Egan DA, Walter K, Holzman TF, Robbins T, Fesik SW. Solution structure of the DNA-binding domain of a human papillomavirus E2 protein: evidence for flexible DNA-binding regions. Biochemistry. 335:1996;2095-2103 This paper describes the solution structure of the DNA binding and dimerization domain of the E2 protein from human papillomavirus as determined by NMR spectroscopy. The structure was very similar to that of the co-crystal structure of the E2 protein from bovine papillomavirus [10] but slight differences in the demerization interface were observed.
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Liang, H.1
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Solution structure of the origin DNA-binding domain of SV40 T-antigen
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of outstanding interest. In this paper the solution structure determination by NMR of the DNA-binding domain of SV40 T antigen was described. The SV40 T antigen has long served as a paradigm for origin-binding proteins and the structure of its DNA binding domain had been long awaited. The overall fold of this domain is novel but structural similarities to E2, EBNA1 and U1A are discussed.
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of outstanding interest Luo X, Sanford DG, Bullock PA, Bachovchin WW. Solution structure of the origin DNA-binding domain of SV40 T-antigen. Nat Struct Biol. 3:1996;1034-1039 In this paper the solution structure determination by NMR of the DNA-binding domain of SV40 T antigen was described. The SV40 T antigen has long served as a paradigm for origin-binding proteins and the structure of its DNA binding domain had been long awaited. The overall fold of this domain is novel but structural similarities to E2, EBNA1 and U1A are discussed.
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