Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids.

Article Details

Citation

Copy to clipboard

Petitpas I, Grune T, Bhattacharya AA, Curry S

Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids.

J Mol Biol. 2001 Dec 14;314(5):955-60.

PubMed ID

11743713 [ View in PubMed

]

Abstract

The primary ligands of human serum albumin (HSA), an abundant plasma protein, are non-esterified fatty acids. In vivo, the majority of fatty acids associated with the protein are unsaturated. We present here the first high-resolution crystal structures of HSA complexed with two important unsaturated fatty acids, the monounsaturated oleic acid (C18:1) and the polyunsaturated arachidonic acid (C20:4). Both compounds are observed to occupy the seven binding sites distributed across the protein that are also bound by medium and long-chain saturated fatty acids. Although C18:1 fatty acid binds each site on HSA in a conformation almost identical with that of the corresponding saturated compound (C18:0), the presence of multiple cis double bonds in C20:4 induces distinct binding configurations at some sites. The observed restriction on binding configurations plausibly accounts for differences in the pattern of binding affinities for the primary sites between polyunsaturated fatty acids and their saturated or monounsaturated counterparts.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Arachidonic Acid	Serum albumin	Protein	Humans	No	Not Available	Details
Oleic Acid	Serum albumin	Protein	Humans	Unknown	Not Available	Details

Polypeptides

Name	UniProt ID
Serum albumin	P02768	Details