Importance of conserved residue in human copper chaperone

Written by Marina Chanidou, Guest Web Writer for Metallomics and PhD student at the University of York.

Understanding copper-binding properties

Copper is one of the most abundant metals in the human body and it takes part in a number of biological processes. Because both copper deficiency and excess can cause serious health problems, copper homeostasis is tightly regulated. Therefore, monitoring the use and transfer of copper in the human body is of great interest to scientists.

To understand how copper is transported into the cells, Changlin Tian and Yangzhong Liu at the University of Science and Technology of China investigated a mutation of copper chaperone Atox1 which affects the conserved residue Lys60. Lys60 plays an important role in the formation of protein heterodimers and determines the copper transfer to the target protein. In their study, the researchers used NMR and protein dynamic studies and indicated that the mutation causes crucial structural changes that affect the metal-binding centres and the protein flexibility. These results indicate that the residue Lys60 preserves the structure and dynamics of Atox1 and thus the protein’s ability to bind copper and deliver it to the target protein.

To know more about this work, please access the link below. This paper will be free to read until November 15th .

Conserved residue modulates copper-binding properties through structural dynamics in human copper chaperone Atox1
Zhaoyong Xi, Chaowei Shi, Changlin Tian and   Yangzhong Liu
Metallomics, 2013, 5, 1566-1573
DOI: 10.1039/C3MT00190C

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No Responses to “Importance of conserved residue in human copper chaperone”

  1. arpit patel says:
    Your comment is awaiting moderation. This is a preview, your comment will be visible after it has been approved.

    Lys60 plays an important role in the formation of protein heterodimers and determines the copper transfer to the target protein. In their study https://upstrackingit.com/, the researchers used NMR and protein dynamic studies and indicated that the mutation causes crucial structural changes that affect the metal-binding centers and protein flexibility.

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