Circulatory zinc transport is controlled by distinct interdomain sites on mammalian albumins.

ABSTRACT: Zinc is an essential nutrient in the body; it is required for the catalytic activity of many hundreds of human enzymes and virtually all biological processes, therefore its homeostasis and trafficking is of crucial interest. Serum albumin is the major carrier of Zn²⁺ in the blood and is required for its systemic distribution. Here we present the first crystal structures of human serum albumin (HSA) and equine serum albumin (ESA) in complex with Zn²⁺. The structures allow unambiguous identification of the major zinc binding site on these two albumins, as well as several further, weaker zinc binding sites. The major site in both HSA and ESA has tetrahedral geometry and comprises three protein ligands from the sidechains of His67, His247 and Asp249 and a water molecule.

SUBMITTER: Handing KB 

PROVIDER: S-EPMC5450522 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature