Fig. 6: Characterization of hIL-1βV47A. | Nature Communications

Fig. 6: Characterization of hIL-1βV47A.

From: Discovery of a selective and biologically active low-molecular weight antagonist of human interleukin-1β

Fig. 6: Characterization of hIL-1βV47A.The alternative text for this image may have been generated using AI.

a Chemical shift differences of backbone 15N and 1H resonances (Supplementary Fig. 9) between wild-type and hIL-1βV47A are mapped in lime green onto the X-ray structure of hIL-1β (salmon; 4DEP31). The isopropyl side-chain of Val47 sits deep in a hydrophobic pocket utilized by ring A of (S)-2 in the crystal structure of its complex with hIL-1β (this work; cyan). b 19F-transverse relaxation experiment (τ = 240 ms) with compound (S)-1 (40 μM) in the absence and presence of hIL-1β and hIL-1βV47A. Signals were scaled to an internal reference. c Binding of (S)-1 to hIL-1βV47A. The protein was titrated with increasing amounts of the compound, and lineshapes were globally fitted to a two-site exchange model (KD = 263 ± 40 μM, koff = 215 ± 47 s−1; N = 2)56.

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