Fatty acid binding to human serum albumin: new insights from crystallographic studies.
Human serum albumin possesses multiple fatty acid binding sites of varying affinities, but the precise locations of these sites have remained elusive. The determination of the crystal structure of human serum albumin complexed with myristic acid recently revealed the positions and architecture of six binding sites on the protein. While the structure of the complex is consistent with a great deal of the biochemical and biophysical data on fatty acid binding, it is not yet possible to provide a completely rigorous correlation between the structural and binding data. The challenge now is to use the new structural information to design experiments that will identify the physiologically important binding sites on HSA and provide a much richer description of fatty acid interactions with the protein.
Curry
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Blackett Laboratory, Imperial College, Prince Consort Road, London, UK. s.curry@ic.ac.uk
Brick
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Franks
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D001665:Binding Sites; D003461:Crystallography; D005227:Fatty Acids / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D012709:Serum Albumin / Q000378:metabolism*
D005227:Fatty Acids; D012709:Serum Albumin