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Title
| - Crystal Structure of the Msx-1 Homeodomain/DNA Complex,
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has manifestation of work
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Author
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Abstract
| - The Msx-1 homeodomain protein plays a crucial role in craniofacial, limb, and nervous systemdevelopment. Homeodomain DNA-binding domains are comprised of 60 amino acids that show a highdegree of evolutionary conservation. We have determined the structure of the Msx-1 homeodomaincomplexed to DNA at 2.2 Å resolution. The structure has an unusually well-ordered N-terminal arm witha unique trajectory across the minor groove of the DNA. DNA specificity conferred by bases flanking thecore TAAT sequence is explained by well ordered water-mediated interactions at Q50. Most interactionsseen 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 indicatea remarkably well-conserved sphere of hydration between the DNA and protein in these complexes.
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is part of this journal
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