Open AccessStructural and Functional Diversity Among the Members of CTR, the Membrane Copper Transporter Family
Author(s) -
Taniya Mandal,
Sumanta Kar,
Saptarshi Maji,
Samarpita Sen,
Arnab Gupta
Publication year - 2020
Publication title -
the journal of membrane biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.591
H-Index - 98
eISSN - 1432-1424
pISSN - 0022-2631
DOI - 10.1007/s00232-020-00139-w
Subject(s) - transporter , copper , homology (biology) , sequence homology , biology , microbiology and biotechnology , biochemistry , genetics , computational biology , chemistry , peptide sequence , gene , organic chemistry
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.