Zinc standard for economy
Article Abstract:
GAL4 DNA-binding domain is a zinc-mediated peptide loop whose interaction with nucleic acids is a fundamental part DNA transcription. The most remarkable feature of the GAL4, which sets it apart from the two previously described zinc-bearing domains, is its metal cluster, which helps it carry out its DNA binding functions. The three types of zinc-binding motif share the role of exposing an alpha helix that lies in the DNA's major groove and controls interactions with the bases of the target sequence.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Dymer, dymer binding tight
Article Abstract:
The DNA-binding domains of ligand-activated transcription factors have been characterized structurally as containing a metal-bearing fold. The structure of ligand-activated factors has been further elucidated by a new study of the human receptor for 9-cis retinoic acid, the results of which showed the crystal structure of the ligand-binding domain which provides the stereochemical explanations for its interactions with various ligands.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Crystal structure of the bacterial membrane protein ToIC central to multidrug efflux and protein export
Article Abstract:
The 2.1-A crystal structure of ToLC from Escherichia coli is reported.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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