Abstract
The human (h)ZIP4 protein is the primary zinc uptake protein in the intestine, the main location of zinc uptake. hZIP4 encodes eight transmembrane domains as well as a large cytosolic domain. The cytosolic domain contains a histidine rich region. Previously, we have demonstrated that two zinc ions can bind to this cytosolic domain in a sequential manner. It has been proposed that zinc binding within the cytosolic domain regulates the surface expression of hZIP4. Here, we have used NMR spectroscopy to quantify the structural characteristics of this cytosolic domain in the absence and presence of zinc.
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