Literature summary for 7.2.2.8 extracted from

Bossak, K.; Drew, S.C.; Stefaniak, E.; Plonka, D.; Bonna, A.; Bal, W.
The Cu(II) affinity of the N-terminus of human copper transporter CTR1 Comparison of human and mouse sequences (2018), J. Inorg. Biochem., 182, 230-237 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O15431	-	-

General Information

General Information	Comment	Organism
physiological function	the N-terminus of CTR1 may serve as intermediate binding site during Cu(II) transfer from blood copper carriers to the transporter. Human N-terminal sequence Met-Asp-His, MDH-amide, but not MNH-amide forms a low abundance complex with non-amino terminal Cu(II)- and Ni(II)-binding site coordination involving the Met amine, His imidazole and Asp carboxylate. This species might assist Cu(II) relay down the peptide chain or its reduction to Cu(I), both necessary for the CTR1 function	Homo sapiens

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Release 2023.1 (January 2023)