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. 2018 Jul 17;24(3):557–568.e5. doi: 10.1016/j.celrep.2018.06.080

Figure 3.

Figure 3

Structural Basis of Molecular Effects of F133L, G213S, V228F, V354A, and S239N Mutants

(A) F133L mutation disrupts a cation-π interaction between F133 and K87.

(B) Modeling the effects of G213S and V228F mutations on the crystal structure of Gαs-AC5 complex (PDB: 1AZS).

(C) G213S mutation introduces hydrogen bond network with γ phosphate of GTPγS (orange) and three P loop residues (olive).

(D) Predicted effects of V228F mutation on the organization of Gαs-AC5 complex.

(E) V354A mutation eliminates a hydrophobic interaction with a guanine ring of a nucleotide (E1). Comparison of wild-type (E2) and V354A (E3) by electrostatic surfaces shows the broadening of nucleotide-binding pocket in the mutant.

(F) S239N mutation introduces a water-mediated hydrogen bond with G51 in a P loop (olive). Please refer to detailed descriptions in the main text.

See also Figure S2.