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Figure 4.
FIGURE 4. Residues of the RyRP12 peptide (residues
3616-3627 or RyR1) and S100A1 involved in Ca^2^+-S100A1-RyRP12
complex formation. A, diagram illustrating hydrophobic residues
involved in the RyRP12-S100A1 interaction including Ala-53,
Ile-57, Leu-77, Ala-80, Leu-81, and Ala-84 of S100A1, and
Trp-3620, Leu-3623, and Leu-3624 of RyRP12. B, ribbon diagram
illustrating hydrophilic residues in the RyRP12-S100A1 complex
that are likely involved in ionic interactions, including Asp-52
and Glu-63 on S100A1 and Lys-3616, Lys-3622, and Lys-3627 on the
RyRP12 peptide. C, space-filling diagram of the S100A1-RyP12
peptide showing residues in green (Trp-3620 and Leu-3624) that
are important for calmodulin binding to the ryanodine receptor.
The rest of the RyRP12 peptide is colored in red, and the S100A1
subunits 1 and 2 are colored tan and blue, respectively. D,
ribbon diagram of the C-terminal region of CaM bound to the
CaMBD of the RyR (residues 3614-3643 of RyR; Protein Data Bank
code 2BCX) (17), showing side chains of the RyR that are
involved in ionic interactions with CaM; these same residues are
also likely to form salt bridges with negatively charged side
chains of Ca^2+-S100A1.
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