1e7f
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HUMAN SERUM ALBUMIN COMPLEXED WITH DODECANOIC ACID (LAURIC ACID)
OverviewOverview
Human serum albumin (HSA) is an abundant plasma protein that is, responsible for the transport of fatty acids. HSA also binds and perturbs, the pharmacokinetics of a wide range of drug compounds. Binding studies, have revealed significant interactions between fatty acid and drug-binding, sites on albumin but high-resolution structural information on ligand, binding to the protein has been lacking. We report here a crystallographic, study of five HSA-fatty acid complexes formed using saturated medium-chain, and long-chain fatty acids (C10:0, C12:0, C14:0, C16:0 and C18:0). A total, of seven binding sites that are occupied by all medium-chain and, long-chain fatty acids have been identified, although medium-chain fatty, acids are found to bind at additional sites on the protein, yielding a, total of 11 distinct binding locations. Comparison of the different, complexes reveals key similarities and significant differences in the, modes of binding, and serves to rationalise much of the biochemical data, on fatty acid interactions with albumin. The two principal drug-binding, sites, in sub-domains IIA and IIIA, are observed to be occupied by fatty, acids and one of them (in IIIA) appears to coincide with a high-affinity, long-chain fatty acid binding site.
DiseaseDisease
Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]
About this StructureAbout this Structure
1E7F is a Single protein structure of sequence from Homo sapiens with DAO as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin., Bhattacharya AA, Grune T, Curry S, J Mol Biol. 2000 Nov 10;303(5):721-32. PMID:11061971
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