Figure 7.
Fig. 7. Model of the complex of C1 and S2Δ. (a) Overview of
the position of C1 (blue) on S2Δ (red). Amino acids in C1 with
chemical shift perturbations larger than angle
bracket Δδ angle
bracket [tot] are marked by green spheres on their N positions.
(b) Detailed view of the interactions of C1 and S2Δ in the
model. C1 is shown in blue, and S2Δ is shown in red. Important
side chains in the interaction are coloured by atom type
(carbon, green; oxygen, red; nitrogen, blue), and labels are
coloured by protein. (c) Depiction of the overall assembly of C1
and C2 and the linker on S2Δ. Domains C1 and C2 of MyBP-C are
shown in orange, and the linker between them is shown in gray.
The three phosphorylation sites in the linker are shown in
purple, residues mutated in FHC are shown in yellow with labels
and charged residues are coloured according to their charge.
S2Δ is shown with solvent-accessible surface coloured by a
simple electrostatic potential with the N-terminus on the left
(hidden by C1) and the C-terminus on the right. The position of
the C-terminal cluster of FHC-related point mutations in S2Δ is
indicated by the residue numbers (924–936).
The above figure is reprinted
from an Open Access publication published by Elsevier:
J Mol Biol
(2008,
384,
615-630)
copyright 2008.
angle
bracket Δδ 
angle
bracket [tot] are marked by green spheres on their N positions.
(b) Detailed view of the interactions of C1 and S2Δ in the
model. C1 is shown in blue, and S2Δ is shown in red. Important
side chains in the interaction are coloured by atom type
(carbon, green; oxygen, red; nitrogen, blue), and labels are
coloured by protein. (c) Depiction of the overall assembly of C1
and C2 and the linker on S2Δ. Domains C1 and C2 of MyBP-C are
shown in orange, and the linker between them is shown in gray.
The three phosphorylation sites in the linker are shown in
purple, residues mutated in FHC are shown in yellow with labels
and charged residues are coloured according to their charge.
S2Δ is shown with solvent-accessible surface coloured by a
simple electrostatic potential with the N-terminus on the left
(hidden by C1) and the C-terminus on the right. The position of
the C-terminal cluster of FHC-related point mutations in S2Δ is
indicated by the residue numbers (924–936).