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. Author manuscript; available in PMC: 2022 Feb 24.
Published in final edited form as: Chem Rev. 2021 Feb 5;121(4):2545–2647. doi: 10.1021/acs.chemrev.0c01122

Figure 28.

Figure 28.

Metal binding sites and post-translational modifications of αS. αS harbors three binding sites for metal ions (displayed with colored circles): the low affinity, nonspecific metal binding site at the acidic DPDNEA segment in the C-terminal, the His50 site, and the first five residues at the N-terminal. His50 can anchor transition-metal ions such as Zn(II), Fe(III), and Fe(II), but the highest affinity is found for Cu(II) and Cu(I) ions. The N-terminus of αS is a high affinity and highly specific site for Cu ions. Reprinted with permission from ref 734. Copyright 2021 John Wiley and Sons.