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Article

A regulated two-step mechanism of TBP binding to DNA: a solvent-exposed surface of TBP inhibits TATA box recognition.

Cell - 8 Mar 2002

Zhao Xuemei, Herr Winship

Abstract excerpt

The TATA box binding protein TBP plays a universally important role in eukaryotic nuclear transcription. By mutagenesis, we have discovered a solvent-exposed surface of the structured TBP core domain that is important for inhibition of the DNA binding and DNA-bending activities of full-length wild-type TBP. Full-length wild-type TBP initially binds the TATA box to form an unstable complex containing unbent DNA,...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 11893333
DOI: 10.1016/s0092-8674(02)00648-7

Genes

TBP

Provenance

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

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A regulated two-step mechanism of TBP binding to DNA: a solvent-exposed surface of TBP inhibits TATA box recognition.PMID 11893333Read ↗

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A new regulatory domain on the TATA-binding protein.Semantic proximity Read ↗

TFIIA changes the conformation of the DNA in TBP/TATA complexes and increases their kinetic stability.Semantic proximity Read ↗

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