Abstract
A model is presented for the structure of the lactose repressor protein and for its interaction with inducer, operator DNA, and nonspecific DNA. The proposed structure is based on experimental evidence from this laboratory and from the literature and is offered as an integration of the available data on this system. Features unique to this model include: (i) interaction of the core region of the protein with the operator, (ii) primary effects of the conformational change in response to inducer on the core-operator interaction, (iii) contacts between all four subunits of the protein and the operator DNA, and (iv) qualitative differences in operator and nonspecific DNA binding.
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