Nullspace Sampling with Holonomic Constraints Reveals Molecular Mechanisms of Protein Gαs
Fig 2
a) The Gαs subunit consists of a Ras-domain and an α-helical domain. Linker I and II are shown in yellow, and the binding site of the nucleotide in between the two domains is indicated by a blue circle. The location of donor and acceptor atoms of the hydrogen bonding network used for KGS are indicated with white (donors) and red (acceptor) spheres. b) The activated state of Gs (pale cyan) superimposed onto the inactive state. Upon activation, the α-helical domain undergoes a large rotational motion. Helix α5 translates and rotates upward to interact with the cytoplasmic core of the receptor.