On the structure and function of apolipoproteins: more than a family of lipid-binding proteins

被引：66

作者：

Bolanos-Garcia, VM ^{[1
]}

Miguel, RN ^{[1
]}

机构：

[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England

来源：

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY | 2003年 / 83卷 / 01期

基金：

英国惠康基金;

关键词：

apolipoprotein structure; lipid-binding proteins; amyloid formation; kinetic stability; amphipathic helices;

D O I：

10.1016/S0079-6107(03)00028-2

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：

Exchangeable apolipoproteins have been the subject of intense biomedical investigation for decades. However, only in recent years the elucidation of the three-dimensional structure reported for several members of the apolipoprotein family has provided insights into their functions at a molecular level for the first time. Moreover, the role of exchangeable apolipoproteins in several cellular events distinct from lipid metabolism has recently been described. This review summarizes these contributions, which have not only allowed the identification of the apolipoprotein domains that determine substrate binding specificity and/or affinity but also the plausible molecular mechanism(s) involved. (C) 2003 Elsevier Science Ltd. All rights reserved.

引用

页码：47 / 68

页数：22

共 115 条

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