Fig. 4: The conformational changes of hPhK after phosphorylation treatment.
From: Molecular basis for the regulation of human phosphorylase kinase by phosphorylation and Ca2+
a Structural comparison of the central β4 tetramer structure of dephosphorylated hPhK and phosphorylated hPhK. The left and right panels show the enlarged views of distance changes between β2/β4 and β1/β2, respectively. dephosphorylated hPhK is colored in light gray, while phosphorylated hPhK is colored according to Fig. 1a. The Loop-27 is depicted in cyan. b Structural comparison of dephosphorylated αβγδ subcomplex (light gray) and phosphorylated αβγδ subcomplex (colored). The red arrow indicates the direction of conformational change. The model in the lower right corner demonstrates the tendency of conformation changes. c Structural comparison of dephosphorylated β subunit (light gray) and phosphorylated β subunit (green). The red arrow indicates the direction of conformational change. The model in the lower right corner demonstrates the tendency of conformation changes. d Interaction details of the Loop-27 from β1 subunit and the adjacent β2 subunit. The β1 and β2 subunits are colored in slateblue and salmon, respectively, while Loop-27 is colored in cyan. Potential hydrogen bonds (black) and salt bridges (red) are indicated by dashed lines. e In the phosphorylated state, the β-subunit Loop-701 is located between the β subunit and the γ-N lobe. Phosphorylation sites are labeled by red balls.
