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. Author manuscript; available in PMC: 2021 Mar 19.
Published in final edited form as: Cell Chem Biol. 2020 Jan 7;27(3):269–282.e5. doi: 10.1016/j.chembiol.2019.12.008

Figure 4: Structural insights into Yck2 as target of GW in C. albicans.

Figure 4:

A, Structure of the Yck2-GW complex. (left) Protein is shown in cartoon representation, GW is shown in ball-and-stick.  Electron density for GW is simulated annealing omit map at 3.0 σ. The amino acids at the N- and C-termini that are resolved in the structure are labeled. (right) Zoomed-in view of the ATP/GW-binding pocket.  Hydrogen bonds are shown as dashed lines. B, Comparison of ATP-binding pockets of Yck2, human CK1α, CK1δ, CK1ε and CK1γ3. Only residues that show sequence/structural differences are shown. Yck2 E52 is part of the glycine-rich loop. The distances between GW and W336 and K342 are indicated. C, Surface representation of theYck2 kinase domain showing GW bound in the ATP-binding pocket and the C-terminal region colored in magenta. (See also Figures S4).