Fatty acid binding to human serum albumin: new insights from crystallographic studies

被引:462
作者
Curry, S [1 ]
Brick, P [1 ]
Franks, NP [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Blackett Lab, London SW7 2BZ, England
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 1999年 / 1441卷 / 2-3期
关键词
human serum albumin; fatty acid; crystal structure;
D O I
10.1016/S1388-1981(99)00148-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:131 / 140
页数:10
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