Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites

Human serum albumin (HSA) is the most abundant protein in the circulatory system. Its principal function is to transport fatty acids, but it is also capable of binding a great variety of metabolites and drugs. Despite intensive efforts, the detailed structural basis of fatty acid binding to HSA has...

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Veröffentlicht in:Nature Structural Biology 1998-09, Vol.5 (9), p.827-835
Hauptverfasser: Curry, Stephen, Mandelkow, Hendrik, Brick, Peter, Franks, Nick
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Sprache:eng
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