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Figure 5.
FIGURE 5. Schematic of S100A1 function in skeletal muscle.
Ca^2+-S100A1 and Ca^2+-CaM bind to an overlapping region of RyR1
(red) in a Ca^2+-dependent manner. S100A1 binding leads to
events that enhance SR calcium release. In contrast, calmodulin
binding to this CaM binding domain leads to events that reduce
SR calcium release. Competition between these two
calcium-binding proteins for this target site may regulate SR
Ca^2+ release in skeletal muscle. The asterisk close to the
Ca^2+-S100A1-RyRP12 structure denotes the location of the
residues of RyR that are C-terminal to RyRP12 (residues
3616-3627 of RyR) present in the longer RyR peptide (residues
3614-3643 of RyR), used for structural studies when bound to CaM.
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