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

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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 b...

Topics

Amino Acid Sequence
Base Sequence
DNA
DNA-Binding Proteins
Magnetic Resonance Spectroscopy
Models, Chemical
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Operator Regions, Genetic
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Repressor Proteins

Solutions

Spectrum Analysis, Raman

Transcription Factors

Viral Proteins

Viral Regulatory and Accessory Proteins

Source

Open in PubMed

Identifiers

PMID: 8144673

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8144673-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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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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