Figure 2

Figure 2

JS (V194A) and JATD (A199P) Mutations in Human CEP120 Cause Subtle Changes in the C2B Domain Structure

(A) Per-residue plot of the weighted chemical shift perturbations of the human CEP120 C2B V194A (left) and A199P mutant (right) relative to the WT protein observed in ¹H,¹⁵N BEST-TROSY NMR spectra at 20°C. Gray bars indicate line-broadened peaks.

(B) Molecular surface representation of the O.n. C2B structure colored by CONSURF conservation scores from cyan (variable) to burgundy (conserved).

(C) Homology model of human CEP120 C2B as ribbon representation. The weighted chemical-shift perturbations of the human CEP120 C2B V194A (left) and A199P mutant (right) relative to the WT protein as observed in (A) are plotted color-coded onto this model.

See also Figures S2 and S3.