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Biological Physics Seminar (CPLC): “Molecular Underpinning of Postsynaptic Calmodulin-dependent Calcium Signaling”

Event Type
Seminar/Symposium
Topic
biophysics
Sponsor
Dr. Martin Gruebele
Location
Loomis 144
Date
Feb 17, 2017   2:00 pm  
Speaker
Dr. Margaret Cheung, Univ. of Houston Dept. of Physics , Rice Univ. Center for Theoretical Biological Physics
Cost
N/A
Contact
Becky McDuffee
E-Mail
mcduffbe@illinois.edu
Phone
217-300-0898
Views
67
Originating Calendar
Physics - Physics of Living Cells Seminar

Calcium (Ca2+) is exquisitely utilized by a cell for transducing external stimuli through its gradient of extracellular (~1000 μM) and intracellular (~0.1 μM) concentration. A broad spectrum of Ca2+ signals are encoded by protein calmodulin (CaM) through specific binding with various targets regulating CaM-dependent Ca2+ signaling pathways in neurons. I will focus on binding between CaM and two specific targets, Ca2+/CaM-dependent protein kinase II (CaMKII) and neurogranin (Ng), as they antagonistically regulate CaM-dependent Ca2+ signaling pathways in neurons. I will show the impact of bound calmodulin (CaM)-target compound structure on the affinity of calcium (Ca2+) by integrating coarse-grained models and all-atomistic simulations with non-equilibrium physics.  We discovered the molecular underpinnings of lowered affinity of Ca2+ for CaM in the presence of Ng by showing that the N-terminal acidic region of Ng peptide pries open the β-sheet structure between the Ca2+ binding loops particularly at C-domain of CaM, enabling Ca2+ release. In contrast, CaMKII peptide increases Ca2+ affinity for the C-domain of CaM by stabilizing the two Ca2+ binding loops. Through distinctive structural differences in the bound complexes of apoCaM-Ng13-49 and holoCaM-CaMKII, CaM’s affinity for Ca2+ is delineated by its progressive mechanism of target binding.

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