Literature DB >> 32975619

Structural and Functional Diversity Among the Members of CTR, the Membrane Copper Transporter Family.

Taniya Mandal1, Sumanta Kar1, Saptarshi Maji1, Samarpita Sen1, Arnab Gupta2.   

Abstract

Copper is crucial for carrying out normal physiological functions in all higher life forms. Copper Transporter 1 (CTR1) is the high-affinity copper importer found in all eukaryotic organisms. The copper transporter family primarily comprises ~ six members (CTR1-6) and the related members share high sequence homology with CTR. However, with the exception of CTR1, not all six CTRs are present in every organism. Despite having a simple trimeric channel structure, CTR1 and other members exhibit some unique regulatory properties. In the present review, we attempt to understand the diversity and similarity of regulation and functioning of the members of this copper transporter family.

Entities:  

Keywords:  CTR; Copper; Copper Transporter

Mesh：

Substances：

Year:  2020        PMID： 32975619      PMCID： PMC7611187          DOI： 10.1007/s00232-020-00139-w

Source DB:  PubMed          Journal:  J Membr Biol        ISSN： 0022-2631            Impact factor:   1.843


  48 in total

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4.  hCTR1: a human gene for copper uptake identified by complementation in yeast.

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8.  Mechanistic comparison of human high-affinity copper transporter 1-mediated transport between copper ion and cisplatin.

Authors:  Zheng D Liang; David Stockton; Niramol Savaraj; Macus Tien Kuo
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Authors:  Stefanie Schwab; Jason Shearer; Steven E Conklin; Bruno Alies; Kathryn L Haas
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Authors:  Christopher J De Feo; Stephen G Aller; Gnana S Siluvai; Ninian J Blackburn; Vinzenz M Unger
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3.  A Deeper Insight in Metal Binding to the hCtr1 N-terminus Fragment: Affinity, Speciation and Binding Mode of Binuclear Cu2+ and Mononuclear Ag+ Complex Species.

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4.  Molecular Interplay at the Membrane and Impact on Cellular Physiology.

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