Crystallization and preliminary X-ray analysis of the NKX2.5 homeodomain in complex with DNA

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):1079-82. doi: 10.1107/S1744309108033447. Epub 2008 Oct 31.

Abstract

As part of an effort to elucidate the molecular basis for the pathogenesis of NKX2.5 mutations in congenital heart disease using X-ray crystallography, the NKX2.5 homeodomain has been crystallized in complex with a specific DNA element, the -242 promoter region of atrial natriuretic factor. Crystals of the homeodomain-DNA complex diffracted X-rays to 1.7 A resolution and belonged to space group P6(5), with unit-cell parameters a = b = 71.5, c = 94.3 A. The asymmetric unit contained two molecules of the NKX2.5 homeodomain and one double-stranded oligonucleotide.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Atrial Natriuretic Factor / genetics
  • Crystallization
  • DNA / chemistry*
  • Homeobox Protein Nkx-2.5
  • Homeodomain Proteins / chemistry*
  • Homeodomain Proteins / genetics
  • Humans
  • Macromolecular Substances / chemistry
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Conformation
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Transcription Factors / chemistry*
  • Transcription Factors / genetics
  • X-Ray Diffraction

Substances

  • Homeobox Protein Nkx-2.5
  • Homeodomain Proteins
  • Macromolecular Substances
  • NKX2-5 protein, human
  • Recombinant Fusion Proteins
  • Transcription Factors
  • Atrial Natriuretic Factor
  • DNA