Structure and function of α-fetoprotein:: a biophysical overview

被引:96
|
作者
Gillespie, JR
Uversky, VN [1 ]
机构
[1] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA
[2] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 142292, Moscow Region, Russia
基金
俄罗斯基础研究基金会;
关键词
alpha-fetoprotein; protein conformation; protein structural property; conformational stability; structure-function relationship; protein denaturation;
D O I
10.1016/S0167-4838(00)00104-7
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
alpha-Fetoprotein (AFP) is a large serum glycoprotein belonging to the intriguing class of once-developmental proteins. AFP has attracted considerable attention since it was shown that the change in its serum level during pregnancy is a hallmark of the development of numerous embryonic disorders, while the increase in its content in the plasma of adults correlates with the appearance of several pathological conditions. Over the past 30 years, some 11 000 papers have been published concerning AFP, an average rate of over a publication a day since 1969. The majority of publications are about the application of the protein in diagnostics, or about other uses of AFP in biomedicine; though some of them describe the biochemical and functional properties of AFP, two aspects have been extensively reviewed. However, surprisingly little is currently known about structural properties of this protein as well as about the molecular mechanism of its function. The present review pursues the aim to describe the current state of the art in studies of structural properties and conformational stability of AFP. An attempt to establish the relationship between conformational transformations in AFP and its function is also made. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:41 / 56
页数:16
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