Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant.

ABSTRACT: Our goal was to compute a stable, full-sequence design of the Drosophila melanogaster engrailed homeodomain. Thermal and chemical denaturation data indicated the design was significantly more stable than was the wild-type protein. The data were also nearly identical to those for a similar, later full-sequence design, which was shown by NMR to adopt the homeodomain fold: a three-helix, globular monomer. However, a 1.65 A crystal structure of the design described here turned out to be of a completely different fold: a four-helix, rodlike tetramer. The crystallization conditions included approximately 25% dioxane, and subsequent experiments by circular dichroism and sedimentation velocity analytical ultracentrifugation indicated that dioxane increases the helicity and oligomerization state of

SUBMITTER: Hom GK 

PROVIDER: S-EPMC2253454 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature