Locating high-affinity fatty acid-binding sites on albumin by x-ray crystallography and NMR spectroscopy.

ABSTRACT: Human serum albumin (HSA) is a versatile transport protein for endogenous compounds and drugs. To evaluate physiologically relevant interactions between ligands for the protein, it is necessary to determine the locations and relative affinities of different ligands for their binding site(s). We present a site-specific investigation of the relative affinities of binding sites on HSA for fatty acids (FA), the primary physiological ligand for the protein. Titration of HSA with [(13)C]carboxyl-labeled FA was used initially to identify three NMR chemical shifts that are associated with high-affinity binding pockets on the protein. To correlate these peaks with FA-binding sites identified from the crystal structures of FA-HSA complexes, HSA mutants were engineered with substitutions of amino aci

SUBMITTER: Simard JR 

PROVIDER: S-EPMC1312385 | biostudies-literature | 2005 Dec

REPOSITORIES: biostudies-literature