Extended Data Figure 2: Consensus secondary structure prediction for rabbit RyR1 generated in SABLE.
From: Architecture and conformational switch mechanism of the ryanodine receptor
Extension of domains is indicated by rectangles colour-coded as in Fig. 1. Except for the N-terminal AB domain and the three SPRY domains located in the first 1,650 residues, RyR1 is predicted to fold mainly in α-helices connected with coiled structures. The 165 amino acid sequence between residues 4,375 and 4,540, connecting the amphipathic region with the transmembrane domain, is glycine- and proline-rich and predicted to be disordered.
