Structure of the cro repressor from bacteriophage λ and its interaction with DNA

Structure of the cro repressor from bacteriophage λ and its interaction with DNA
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λ噬菌体cro阻遏物的结构及其与DNA的相互作用

DOI:
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发表时间:
1981
期刊:
影响因子:
64.8
通讯作者:
B. W. Matthews
B. W. Matthews
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Wayne F. Anderson;Wayne F. Anderson;D. Ohlendorf;Y. Takeda;B. W. Matthews

文献摘要

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The three-dimensional structure of the 66-amino acid cro repressor protein of bacteriophage λ suggests how it binds to its operator DNA. We propose that a dimer of cro protein is bound to the B-form of DNA with the 2-fold axis of the dimer coincident with the 2-fold axis of DNA. A pair of 2-fold-related α-helices of the represser, lying within successive major grooves of the DNA, seem to be a major determinant in recognition and binding. In addition, the C-terminal residues of the protein, some of which are disordered in the absence of DNA, appear to contribute to the binding.