Thus the data presented here suggest that the kinase domain conformation, controlled by three specific tyrosines, and the folding of the C-terminal region, including the FABD, are key determinants in the regulation of the BCR-ABL NLS function.
In a straightforward scenario, oligomerization of STIM1 likely helps to extend its C-terminal conformation controlled by domains within the first and third coiled-coil regions.
Nevertheless, conformation controls should be included to ensure that changes in FRET are reflective of differences in mechanical tension and not κ artifacts.
The so-called activation segment, whose conformation controls catalytic activity and access to the substrate binding pocket, can undergo a large conformational change with the active state assuming a 'DFG-in' and an inactive state assuming a 'DFG-out' conformation.
IMPDHs that are resistant to mycophenolic acid have high values of k cat, which indicates that the equilibrium between open and closed conformations controls both inhibition and the catalytic cycle (13).
Developmentally variable chromatin conformation can control protein access to these sites and can regulate transcription.
Together, these results suggest that autophosphorylation occurring at specific tyrosines in the SH2-kinase linker (Y232) and the kinase P-loop (Y253, 257) can affect the N-lobe conformation, which controls the NLS function.
Another tier of chromatin conformation is controlled by nucleosome remodelling complexes including the SWI/SNF family [ 18].
Over the past decade evidence has mounted in favor of the hypothesis that stem cell self-renewal is regulated through heterochromatin conformation under the control of PcG protein complexes.
Given the high number of possible glycans attached to proteins, manifold functions can be attributed to the carbohydrate moiety: folding, stability, conformation, solubility, quality control, half-life, oligomerization or functionality.
Molecular docking study of studied compounds (1, 8, 9, 10) against anticancer targets aromatase (PDB: 3EQM), quinone reductase (PDB: 3G5M) showed active conformations comparable to control molecule.
