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Figure 1.
Figure 1. The RYR1 Target Presents Hydrophobic Anchors on
Opposite Faces of a Helix
(A) Alignment of CaM binding-site
residues 3614–3643 of human RYR1 with rat and zebrafish RYR1
sequences and human RYR2 and RYR3 sequences. Residues identical
in at least four sequences are in boldface.
(B) Electron
density for the target peptide is well defined. Stereo pair of
electron density from the final 2F[o] − F[c] composite omit
map, contoured at 1.5 σ, at the target peptide
(Trp3621–Arg3630). The final model is superimposed on the map.
(C) The 1-17 anchor spacing positions the lobes of CaM on
opposite sides of the helical target. Two views of a ribbon
diagram representation of the Ca^2+CaM/RYR1 peptide complex. CaM
is drawn in blue, the RYR1 peptide in white, and the four
calcium atoms are shown in red. The side chains of the RYR1
hydrophobic residues that anchor the two lobes of CaM are shown
as sticks. Images were generated in PyMOL (DeLano Scientific).
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