Crystallization and preliminary studies of the DNA-binding runt domain of AML1

Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):269-71. doi: 10.1107/s0907444900015791.

Abstract

The acute myeloid leukaemia 1 (AML1) protein belongs to the Runx family of transcription factors and is crucial for haematopoietic development. The genes encoding Runx1 and its associated factor CBF beta are the most frequent targets for chromosomal rearrangements in acute human leukaemias. In addition, point mutations of Runx1 in acute leukaemias and in the familial platelet disorder FPD/AML cluster within the evolutionary conserved runt domain that binds both DNA and CBF beta. Here, the crystallization of the Runx1 runt domain is reported. Crystals belong to space groups C2 and R32 and diffract to 1.7 and 2.0 A resolution, respectively.

MeSH terms

  • Amino Acid Substitution
  • Animals
  • Binding Sites
  • Core Binding Factor Alpha 2 Subunit
  • Crystallization
  • Crystallography, X-Ray
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / isolation & purification
  • Humans
  • Leukemia / genetics
  • Mice
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / isolation & purification
  • Recombinant Proteins / chemistry
  • Transcription Factors / chemistry*
  • Transcription Factors / genetics
  • Transcription Factors / isolation & purification

Substances

  • Core Binding Factor Alpha 2 Subunit
  • DNA-Binding Proteins
  • Proto-Oncogene Proteins
  • RUNX1 protein, human
  • Recombinant Proteins
  • Runx1 protein, mouse
  • Transcription Factors