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![[Figure 6]](lv5073fig6mag.jpg)
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Figure 6
The central helix and its mutations. (a) Position of the central helix amidst the A (blue), B (green) and C (red) domains. Conformation of the most important amino acids is shown. The ribbon of the central helix is colour-coded by the properties of the respective amino acids: blue, positively charged; red, negatively charged; purple, polar; green, hydrophobic. (b) Central helix residues susceptible to mutations associated with cardiac arrhythmias in the hRyR21–606 structure. (c) The important amino acids forming a charge network stabilizing the structure. Right inset: the two most probable conformations of Phe419 in the I419F mutant (rotamers r1 and r2) show clashes with neighbouring residues, explaining the thermal stability decrease of the structure. Left inset: Arg420 points to solution; this may also occur for R420W in the mutant, explaining why this mutation has not affected the thermal stability. The closest contacts of Trp420 in the R420W mutant are with the Phe424 side chain (≃2.5 Å) and the Thr302 main chain (≃3 Å). Central helix amino-acid residues undergoing mutations are coloured as follows: blue, positively charged; red, negatively charged; purple, polar; green, hydrophobic. |
![[Figure 6]](lv5073fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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