Fig. 3: R420Q/W mutations induce NTD-B domain rotation.
From: Structural basis for ryanodine receptor type 2 leak in heart failure and arrhythmogenic disorders
a–c Aligned models focused on the NTD-B domain of closed PKA-phosphorylated RyR2 (PDB:7U9Q, gray), open PKA-phosphorylated RyR2 (PDB:7U9R, yellow, a), primed PKA-phosphorylated RyR2-R420Q (PDB:8UXC, magenta, b), and primed PKA-phosphorylated RyR2-R420W (PDB:8UXF, magenta, c). Models were aligned at the NSol domain. Conformational changes are indicated with arrows. d–f The same models with overlapping cryo-EM maps around residue 420 of closed PKA-phosphorylated RyR2 (d), primed PKA-phosphorylated RyR2-R420Q (e), and primed PKA-phosphorylated RyR2-R420W (f). R420 interacts with R298 and V300, generating a network of stabilizing interactions. The presence of smaller residues in the mutants leads to the collapse of the 298-303 loop. Conformational changes of the 298-303 loop are indicated using arrows, and distances are provided.
