Crystal structure of the Msx-1 homeodomain/DNA complex.
The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous system development. Homeodomain DNA-binding domains are comprised of 60 amino acids that show a high degree of evolutionary conservation. We have determined the structure of the Msx-1 homeodomain complexed to DNA at 2.2 A resolution. The structure has an unusually well-ordered N-terminal arm with a unique trajectory across the minor groove of the DNA. DNA specificity conferred by bases flanking the core TAAT sequence is explained by well ordered water-mediated interactions at Q50. Most interactions seen at the TAAT sequence are typical of the interactions seen in other homeodomain structures. Comparison of the Msx-1-HD structure to all other high resolution HD-DNA complex structures indicate a remarkably well-conserved sphere of hydration between the DNA and protein in these complexes.
Hovde
S
S
Michigan State University Chemistry Department, East Lansing Michigan 48824, USA.
Abate-Shen
C
C
Geiger
J H
JH
D000595:Amino Acid Sequence; D001483:Base Sequence; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry*; D018398:Homeodomain Proteins / Q000737:chemistry*; D051957:MSX1 Transcription Factor; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors
D018398:Homeodomain Proteins; D051957:MSX1 Transcription Factor; D014157:Transcription Factors; D004247:DNA