Molecular Mechanism of DREAM Dimerization and Interactions with a Non-physiological Ligand Zn2+.
Master of Science (MS)
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DREAM, Neuronal calcium sensors, CBP
Date of Defense
Downstream Regulatory Element Antagonist Modulator (DREAM) belongs to the family of neuronal calcium sensor proteins and it is involved in several processes in the brain.
Zinc has been shown to bind to recoverin, with submillimolar affinity. Based on the high sequence homology between the NCS family, it is proposed that DREAM can also serve as an intracellular target for Zn2+. Fluorescence and CD studies confirm that zinc binds to DREAM with a of Kd = 4 µM, triggering changes in the proteins’ tertiary structure.
The calcium association to DREAM leads to the formation of a Ca2+ bound dimer, while in the apo state, a monomer-tetramer equilibrium was observed. A chimeric version of DREAM was prepared by mutating the residues involved in dimerization. DREAM-NCS1 properties were investigated using spectroscopic techniques. These results point towards the role of hydrophobic interactions and salt bridges in stabilizing the dimer and propagating allosteric signals.
Santiago Estevez, Maria D., "Molecular Mechanism of DREAM Dimerization and Interactions with a Non-physiological Ligand Zn2+." (2019). FIU Electronic Theses and Dissertations. 4320.
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