Fig. 7.
Analysis of structure and intrinsic disorder predisposition of human Gαs subunit. a Multiple structure alignment of free Gαs subunit (red; PDB ID: 6AU6 [136]) and Gαs subunit complexed with the calcitonin receptor, nanobody-35, and the Gβγ dimer (blue; PDB ID: 5UZ7 [122], note that only structure of the Gαs subunit is presented here). Multiple structural alignment was conducted using MultiProt algorithm [225]. b Intrinsic disorder propensity and some important disorder-related functional information generated for human Gαs subunit by the D2P2 database (http://d2p2.pro/), that uses outputs of several disorder predictors (see differently colored bars at the top of the plot), such as ESpritz_DisProt, ESpritz_X-ray, and ESpritz_NMR (shown as ESpritz-D, ESpritz-X, and ESpritz-N, respectively), IUPred_long and IUPred_short (shown as IUPred-l and IUPred-s, respectively), PV2, PrDOS, PONDR® VSL2B, and PONDR® VLXT. This is complemented by the information on the location of domains predicted by Superfamily and Pfam platforms (http://supfam.org/SUPERFAMILY/ and https://pfam.xfam.org/, respectively). The level of agreement between all of the disorder predictors is shown in the middle of the plot as color intensity in an aligned gradient. The green segments represent disorder that is not found within a predicted domain, whereas the blue segments are where the disorder predictions intersect the domain prediction. Positions of disorder-based interactions sites (MoRFs) and sites of curated posttranslational modifications (phosphorylation and ubiquitination) are shown by yellow blocks with zigzag infill and by red and purple circles, respectively