Journal Article10.1006/JMBI.1996.0105
Computer-aided discrimination between active and inactive mutants of the n-terminal domain of the bacteriophage lambda repressor
David C. Kombo,David C. Kombo,George Némethy,George Némethy,Kenneth D. Gibson,Kenneth D. Gibson,S. Rackovsky,S. Rackovsky,Harold A. Scheraga,Harold A. Scheraga +9 more
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TL;DR: It is found that the relative orientation of the fifth helices for active mutants is very similar to the wild-type, and that a unique specific orientation pattern of helix-5 relative to helx-5' is required for dimerization-coupled DNA binding activity.
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About: This article is published in Journal of Molecular Biology. The article was published on 01 Mar 1996. The article focuses on the topics: Helix-turn-helix & B3 domain.
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Citations
One nanosecond molecular dynamics simulation of the N‐terminal domain of the λ repressor protein
TL;DR: Many amino acid residues, including those involved in DNA recognition, undergo a simultaneous transition in their side-chain conformations, consistent with the relationship between side- chain conformation and secondary structural elements, as observed in protein crystal structures.
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A comparative three-dimensional model of the carboxy-terminal domain of the lambda repressor and its use to build intact repressor tetramer models bound to adjacent operator sites
TL;DR: In this paper, a tetrameric model for residues 93-236 of the λ repressor (1gfx) was predicted, based on the UmuD′ crystal structure, as part of four intact repressor molecules bound to two adjacent operator sites.
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An aromatic stacking interaction between subunits helps mediate DNA sequence specificity: operator site discrimination by phage λ cI repressor
TL;DR: The pattern of these effects suggests that the geometry of the face-to-face aromatic stacking interaction between symmetrically related Tyr88 in each subunit, a group in the dimer interface but far removed from the DNA binding interface, plays a critical role in operator discrimination.
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Effects on protein structure and function of replacing tryptophan with 5-hydroxytryptophan: single-tryptophan mutants of the N-terminal domain of the bacteriophage lambda repressor.
TL;DR: The results suggest that replacement of Trp by its analog 5-hydroxyTrp may be tolerated in anα-helix, and this hypothesis is tested in the fifth helices of two functionally active mutants of the N-terminal domain of the bacteriophage λ repressor.
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