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Figure 9 | BMC Biochemistry

Figure 9

From: Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and function

Figure 9

Mapping of the interaction surface involved in the Zn2+Ca2+-S100A12 complex formation using NMR chemical shift perturbations. (A) Overlay of the 1H{15N}-HSQC spectra of [U-, 15N] Ca2+-S100A12 (black) and [U-, 15N] Zn2+, Ca2+-S100A12 (red) shows that 54 out of 80 amide peaks do not significantly change their position upon addition of Zn2+ to Ca2+-s100a12. Significant spectral broadening of the Zn2+, Ca2+-S100A12 peaks is due to the increased molecular weight of the oligomer. (B) Amino acids of the Zn2+, Ca2+-S100A12, whose amide peaks are either completely broadened or underwent large (> 0.1 ppm) chemical shift change, are mapped onto the backbone of crystal structure of the Cu2+, Ca2+-S100A12 dimer (PDB code 1ODB. They are shown in red and cluster around Cu2+ binding motif suggesting that this motif is also involved in Zn2+-binding. Amino acids that are not involved in Zn2+-binding are shown in cyan.

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