Enhanced stability of Cu2+–ATCUN complexes under physiologically relevant conditions by insertion of structurally bulky and hydrophobic amino acid residues into the ATCUN motif-Reference-Cited by-同舟云学术

Enhanced stability of Cu2+–ATCUN complexes under physiologically relevant conditions by insertion of structurally bulky and hydrophobic amino acid residues into the ATCUN motif

Published:2016 Issue:23 Volume:45 Page:9436-9445
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Miyamoto Takaaki¹²³⁴⁵,Fukino Yuta¹²³⁴⁵,Kamino Shinichiro¹²³⁴⁵,Ueda Masashi¹²³⁴⁵^ORCID,Enomoto Shuichi¹²³⁴⁵

Affiliation:

1. Graduate School of Medicine

2. Dentistry

3. and Pharmaceutical Sciences

4. Okayama University

5. Okayama 700-8530

Abstract

The stability of Cu²⁺–ATCUN complexes under physiologically relevant conditions is enhanced by inserting bulky and hydrophobic residues at positions 1 and 2 of the ATCUN peptide.

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/DT/C6DT01387B

Reference63 articles.

1. Amino Terminal Cu(II)- and Ni(II)-Binding (ATCUN) Motif of Proteins and Peptides: Metal Binding, DNA Cleavage, and Other Properties

2. Neuromedin C Binds Cu(II) and Ni(II) via the ATCUN Motif: Implications for the CNS and Cancer Growth

3. NMR structure of neuromedin C, a neurotransmitter with an amino terminal CuII-, NiII-binding (ATCUN) motif

4. Histatins: salivary peptides with copper(II)- and zinc(II)-binding motifs

5. Model Peptides Provide New Insights into the Role of Histidine Residues as Potential Ligands in Human Cellular Copper Acquisition via Ctr1

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