Fig. 5: Cysteines 1078 and 2991 face one another at the neighboring subunits of hRyR2 and are accessible for oxidation depending on channel conformation. | Nature Communications

Fig. 5: Cysteines 1078 and 2991 face one another at the neighboring subunits of hRyR2 and are accessible for oxidation depending on channel conformation.

From: Cysteines 1078 and 2991 cross-linking plays a critical role in redox regulation of cardiac ryanodine receptor (RyR)

Fig. 5

a Suggested localization of cysteines 1078 and 2991 in the 3D cryo-EM model of the closed hRyR2 (PDB ID: 7UA5). Helical domain 2 is shown in cyan. P1 and P2 domains are shown in magenta and orange, respectively. SPRY1 and SPRY2 domains are shown in slate and marine, respectively. The cross-linking cysteines 1078 and 2991 are shown in green. The right panel illustrates the local environments of C1078 and C2991 in closed (PDB ID: 7UA5) and open (PDB ID: 7UA9) conformations. The number in the square brackets represents the cysteine thiol group’s solvent-accessible surface area (ASA) in Å2. Black dashed lines between residue side chains represent the van der Waals interactions, and green dashed lines represent hydrogen bonds. b Localization of cysteines 1078 and 2991 on the primary hRyR2 structure and a potential site of the disulfide formation caused by oxidative stress.

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