Fig. 1
From: Metallothionein-3 as a multifunctional player in the control of cellular processes and diseases
Schematic diagram of MT3 amino acid sequences and structure and its response to oxidative stress. a Amino acid sequences alignments of human MT1, MT2, MT3, and MT4. Conserved cysteine residues are highlighted in dark green. The distinctive sequence differences of MT3 from other MTs include an insertion of Thr5, a conservative CPCP (6–9) sequences, and insertion of the charged hexapeptide EAAEAE (55–60). b Simplified structure of MT3. The β-domain of the N-terminal contains nine cysteine residues, but α-domain of the C-terminal contains 11 cysteine residues, providing three and four zinc binding sites, respectively. c Metal swap in MT3 under oxidative injury. MT3 without any metals (apo-MT3) can bind up to seven zinc. Under ROS or NO stress, three Zn in β-domain can be released by swapping with radicals and the metal exchange ability may protect cells from the oxidative injury