Structural characterization of new deoxycytidine kinase inhibitors rationalizes the affinity-determining moieties of the molecules

Nomme, J.; Murphy, J.M.; Su, Y.; Sansone, N.D.; Armijo, A.L.; Olson, S.T.; Radu, C.; Lavie, A.

doi:10.1107/S1399004713025030

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 6
Determination of K_i^app values better reflects the potency of the inhibitor compared with IC₅₀^app values. (a) Steady-state data and curve fit with the explicit binding model for the four inhibitors. (b) K_i^app, error and coefficient of determination (R²). The fit to the explicit model (providing K_i^app values) is superior to the simplistic fit that determines IC₅₀^app values, and notably reveals that the inhibition is improved with increased alkyl-chain length at the 5-position of the thiazole ring.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 1| December 2014| Pages 68-78

doi:10.1107/S1399004713025030

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