Three-Dimensional Domain Swapping Changes the Folding Mechanism of the Forkhead Domain of FoxP1.

ABSTRACT: The forkhead family of transcription factors (Fox) controls gene transcription during key processes such as regulation of metabolism, embryogenesis, and immunity. Structurally, Fox proteins feature a conserved DNA-binding domain known as forkhead. Interestingly, solved forkhead structures of members from the P subfamily (FoxP) show that they can oligomerize by three-dimensional domain swapping, whereby structural elements are exchanged between adjacent subunits, leading to an intertwined dimer. Recent evidence has largely stressed the biological relevance of domain swapping in FoxP, as several disease-causing mutations have been related to impairment of this process. Here, we explore the equilibrium folding and binding mechanism of the forkhead domain of wild-type FoxP1, and of two mutants

SUBMITTER: Medina E 

PROVIDER: S-EPMC4922571 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature