The C-Terminal Segment of Yeast BMH Proteins Exhibits Different Structure Compared to Other 14-3-3 Protein Isoforms
2010
Abstract
We have investigated the conformational behavior of the C-terminal segment of BMH proteins using the array of biophysical techniques: dynamic light scattering, sedimentation velocity, sedimentation equilibrium, time-resolved fluorescence anisotropy decay, and size exclusion chromatography measurements. We showed that the C-terminal segment of BMH proteins adopts a widely opened and extended conformation that makes difficult its folding into the ligand binding groove, thus increasing the apparent molecular size.
It seems, therefore, that the C-terminal segment of BMH proteins does not function as an autoinhibitor.