Structural Studies of the PU.l Transcription Factor.

Abstract

Ets transcription factors play a role in development and are implicated in some malignant processes. Recently, members of this large gene family have been identified in normal gene expression in mammary cells and also in breast cancer cell lines. In these studies, the crystal structure of the DNA-binding domain of the PU.1 ets protein complexed to DNA has been determined at 2.1 A resolution. The DNA binding domain is a conserved region that binds the core sequence 5'-GGAA/T-3'. The PU.1 domain binds DNA using a loop-helix-loop motif involving conserved amino acids and bases. In this project we have also used nuclear magnetic resonance (NMR) to determine the unbound structure of the domain in solution. The two structures were correlated to understand the process of DNA recognition by ets proteins.

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Document Details

Document Type
Technical Report
Publication Date
Oct 01, 1997
Accession Number
ADA346200

Entities

People

  • Katkathryn R. Ely

Organizations

  • Sanford Burnham Prebys Medical Discovery Institute

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Breast Cancer
  • Cells
  • Chemical Synthesis
  • Chemistry
  • Crystal Lattices
  • Crystal Structure
  • Crystals
  • Gene Expression
  • Magnetic Resonance
  • Molecules
  • Neoplasms
  • Nuclear Magnetic Resonance
  • Proteins
  • Recognition
  • Resonance
  • Transcription Factors

Fields of Study

  • Chemistry

Readers

  • Molecular Biology and Genetics
  • Molecular Genetics