| Forkhead Box Protein P3 (FOXP3) is essential for the development and maintenance of regulatory T cells (Treg) via regulating the expression of genes involved in TCR signaling. Studies of the homologue of FOXP3, FOXP2, demonstrated that FOXP3 might function as a dimer. However, few papers report the structure of FOXP3 especially its conformation in the solution. In this study, hFOXP3S containing a zinc-finger, a leucine zipper and a forkhead domain, was present as various oligomers in solution. Light scattering assay suggested that the zinc finger affects the conformation of oligomers and the precipitation of the protein was due to the aggregation of large oligomers. DSS is able to crosslink homodimers of hFOXP3S and forkhead FOXP3, but domain-swapping exchange between hFOXP3S and forkhead FOXP3 is not observed. The polydispersity of hFOXP3 solution brings plenty of information for the advanced structural research of FOXP3. |
