 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 8]](kw5076fig8mag.jpg)
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Figure 8
F-series compounds show different occupancies. (a) Stereoview of F1 (green), F2 (cyan), F3 (orange) and F4 (yellow) compounds after overlaying the corresponding dCK–F-series structures. The colored arrows indicate the component (hydrogen, methyl, ethyl and propyl) at the 5-position of the thiazole ring. The dotted line indicates the F3-P2 molecule observed with partial occupancy. Gln97 interacting with P1 molecules is also represented. (b) Enlargement of the P2 molecules and stereoview representation of the overlaid inhibitors. The position of Tyr86 depends on the number of inhibitor molecules in the active site. Tyr86 faces downwards to accommodate two molecules of F1 and F2. In the dCK–F3 structure, because of the partial occupancy of the P2 molecule, Tyr86 displays two conformations (represented as dashed bonds) that are related by the black arrow. In contrast, Ty86 fully rotates ∼90° and faces upwards to occupy the space of the missing F4-P2 molecule. (c) The dCK nucleoside-binding site is flexible. The dCK–F1 (green ribbon) and dCK–F4 (yellow ribbon) structures are overlaid. Gray areas highlight the main conformational changes upon binding of one or two inhibitor molecules in the active site of dCK. (i) The black arrow relates the two positions Tyr86 can adopt. (ii) The other main change occurs in the loop spanning residues 200–210. Indeed, this loop moves back (green color) when two inhibitor molecules are bound to dCK. |
![[Figure 8]](kw5076fig8.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
