Crystallization and preliminary X-ray analysis of the NKX2.5 homeodomain in complex with DNA.
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.
Genis
Caroli
C
Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA.
Scone
Peyton
P
Kasahara
Hideko
H
Nam
Hyun Joo
HJ
D000818:Animals; D009320:Atrial Natriuretic Factor / Q000235:genetics; D003460:Crystallization; D004247:DNA / Q000737:chemistry*; D000072576:Homeobox Protein Nkx-2.5; D018398:Homeodomain Proteins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D046911:Macromolecular Substances / Q000737:chemistry; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D000072576:Homeobox Protein Nkx-2.5; D018398:Homeodomain Proteins; D046911:Macromolecular Substances; C095552:NKX2-5 protein, human; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D009320:Atrial Natriuretic Factor; D004247:DNA