Kinetics and thermodynamics of metal binding to the N-terminus of a human copper transporter, hCTR1
Kinetics and thermodynamics of metal binding to the N-terminus of a human copper transporter, hCTR1
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DOI：
10.1039/c3cc45360j
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发表时间：
2013-01-01
影响因子：
4.9
通讯作者：
Sun, Hongzhe
中科院分区：
文献类型：
--
作者：
Du, Xiubo;Li, Hongyan;Sun, Hongzhe
hCTR 1的N-末端被证明通过其富含Met的基序与三个Cu+离子紧密结合（logK = 14.92）并且可逆地结合。Ag+以相同的化学计量比与蛋白质结合，但亲和力比Cu+低得多。该蛋白还通过其ATCUN基序和具有较低亲和力的富含His的基序与两个Cu 2+离子配位。这项研究提供了一个深入了解转运蛋白的选择性。
The N-terminus of hCTR1 was demonstrated to bind three Cu+ ions tightly (logK = 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 Cu2+ ions through its ATCUN motif and His-rich motif with lower affinity. This study provides an insight into the selectivity of the transporter.