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Article

An altered specificity mutation in the lambda repressor induces global reorganization of the protein-DNA interface.

The Journal of biological chemistry - 8 Apr 1994

Benevides J M, Weiss M A, Thomas G J

Abstract excerpt

The lambda repressor exhibits structural characteristics of lock and key complementary through the helix-turn-helix motif, and of induced fit by virtue of DNA-dependent folding of the N-terminal arm. In both cases, molecular recognition is mediated by direct contacts between amino acids and DNA bases. The extent to which such contacts function as discrete elements in a protein-DNA recognition code is not known....

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PMID: 8144673

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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An altered specificity mutation in the lambda repressor induces global reorganization of the protein-DNA interface.PMID 8144673Read ↗

Design of the helix-turn-helix motif: nonlocal effects of quaternary structure in DNA recognition investigated by laser Raman spectroscopy.Semantic proximity Read ↗

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The DNA binding arm of lambda repressor: critical contacts from a flexible region.Semantic proximity Read ↗

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Structural and energetic consequences of disruptive mutations in a protein core.Semantic proximity Read ↗

Isolation of lambda repressor mutants with defects in cooperative operator binding.Semantic proximity Read ↗

Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules.Semantic proximity Read ↗

31P nuclear magnetic resonance spectra and dissociation constants of lac repressor headpiece.duplex operator complexes: the importance of phosphate backbone flexibility in protein.DNA recognition.Semantic proximity Read ↗

Altered specificity in DNA binding by the lac repressor: a mutant lac headpiece that mimics the gal repressor.Semantic proximity Read ↗

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