Human serum albumin or HSA is one of the major types of proteins that are present in the plasma composition. It is such abundant that its concentration on a common blood sample is 5 grams per 100 milliliters. Due to its high concentration in plasma as well as its physiological and pharmaceutical features, it has been subjected to several studies to determine its 3D structure, function, domains, important binding sites, and diseases. The primary structure of HSA describes a single polypeptide with 585 amino acids with the characteristics of having 17 pairs of disulfide bridges, one free cysteine [1]. It has been discovered that there are highly conserved sequences between bovine, human and rat albumins such as Trp-212, 143-155 and 244-263 sequence [2]. It is composed of three domains at positions 19-210, 211-403, and 404-601 with two subdomains each (Ia&b, IIa&b, and IIIa&b). The subcellular location of these protein is the extracellular region on the outside of the cell membrane or secreted. There are 11 metal binding sites, including 1 copper site, 7 calcium sites, 3 zinc sites, additionally, 1 binding site for bilirubin and 1 site for aspirin-acetylated lysine [3].
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Structural highlights
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