Journal
IUBMB LIFE
Volume 57, Issue 12, Pages 787-796Publisher
WILEY
DOI: 10.1080/15216540500404093
Keywords
human serum albumin; structural aspects; ligand binding properties; allostery
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Funding
- Wellcome Trust Funding Source: Medline
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Human serum albumin (HSA), the most prominent protein in plasma, binds different classes of ligands at multiple sites. HSA provides a depot for many compounds, affects pharmacokinetics of many drugs, holds some ligands in a strained orientation providing their metabolic modi. cation, renders potential toxins harmless transporting them to disposal sites, accounts for most of the antioxidant capacity of human serum, and acts as a NO-carrier. The globular domain structural organization of monomeric HSA is at the root of its allosteric properties which are reminiscent of those of multimeric proteins. Here, structural, functional, biotechnological, and biomedical aspects of ligand binding to HSA are summarized.
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