Literature DB >> 9032054

Lac repressor-operator complex.

M A Kercher1, P Lu, M Lewis.   

Abstract

For many years the lac operon of Escherichia coli has been the paradigm for gene regulation. Recently, the structures of the lac repressor core bound to isopropyl-beta-D-1-thiogalactoside (IPTG), the intact apo lac repressor, the intact lac repressor complexes with IPTG and a 21-base-pair symmetric operator, and the refined headpiece of the repressor have been determined. These structures have provided a framework for understanding a wealth of biochemical and genetic information. An analysis of these structures, as well as a description of their function and a comparison to homologous proteins, is now possible.

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Year:  1997        PMID: 9032054     DOI: 10.1016/s0959-440x(97)80010-3

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  11 in total

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6.  The mechanism and high-free-energy transition state of lac repressor-lac operator interaction.

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7.  In situ imaging and isolation of proteins using dsDNA oligonucleotides.

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8.  DNA linking number change induced by sequence-specific DNA-binding proteins.

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9.  Structure, function, and tethering of DNA-binding domains in σ⁵⁴ transcriptional activators.

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Review 10.  An overview of the structures of protein-DNA complexes.

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