Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility.

doi:10.1101/gad.11.2.198

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Article

Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility.

Genes & development - 15 Jan 1997

Jacobson E M, Li P, Leon-del-Rio A, Rosenfeld M G, Aggarwal A K

Abstract excerpt

Pit-1, a member of the POU domain family of transcription factors, characterized by a bipartite DNA-binding domain, serves critical developmental functions based on binding to diverse DNA elements in its target genes. Here we report a high resolution X-ray analysis of the Pit-1 POU domain bound t...

Topics

Amino Acid Sequence
Animals
Base Composition
Base Sequence
Crystallography, X-Ray
DNA
DNA-Binding Proteins
Dimerization
Homeodomain Proteins
Host Cell Factor C1
Humans
Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Molecular Sequence Data

Mutation

Nucleic Acid Conformation

Octamer Transcription Factor-1

POU Domain Factors

Source

Open in PubMed

Identifiers

PMID: 9009203
DOI: 10.1101/gad.11.2.198

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9009203-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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