title: Kinetics and thermodynamics of metal binding to the N-terminus of a human copper transporter, hCTR1.
abstract: The N-terminus of hCTR1 was demonstrated to bind three Cu(+) ions tightly (log K = 14.92) and reversibly via its Met-rich motifs. Ag(+) binds to the protein with the same stoichiometry but much lower affinities than Cu(+). The protein also coordinates two Cu(2+) ions through its ATCUN motif and His-rich motif with lower affinity. This study provides an insight into the selectivity of the transporter.
authors: Department of Chemistry, The University of Hong Kong, Hong Kong, China. hsun@hku.hk.
authors: Xiubo
authors: X
authors: Du
authors: Hongyan
authors: H
authors: Li
authors: Xinghao
authors: X
authors: Wang
authors: Qiong
authors: Q
authors: Liu
authors: Jiazuan
authors: J
authors: Ni
authors: Hongzhe
authors: H
authors: Sun
mesh_terms: D020816:Amino Acid Motifs; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D003300:Copper / Q000737:chemistry*; D000079923:Copper Transporter 1; D006801:Humans; D007477:Ions / Q000737:chemistry; D007700:Kinetics; D011485:Protein Binding; D012834:Silver / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D027682:Cation Transport Proteins; D000079923:Copper Transporter 1; D007477:Ions; C490079:SLC31A1 protein, human; D012834:Silver; D003300:Copper