Study of chaperone-like activity of human haptoglobin:: Conformational changes under heat shock conditions and localization of interaction sites

被引：22
|
作者：
Ettrich, R
Brandt, W
Kopecky, V
Baumruk, V
Hofbauerová, K
Pavlícek, Z
机构：
[1] Charles Univ, Dept Phys & Macromol Chem, CZ-12840 Prague 2, Czech Republic
[2] Inst Phys Biol, CZ-37333 Nove Hrady, Czech Republic
[3] Charles Univ, Dept Biochem, CZ-12840 Prague 2, Czech Republic
[4] Inst Plant Biochem, D-06120 Halle Saale, Germany
[5] Charles Univ, Inst Phys, CZ-12116 Prague 2, Czech Republic
来源：
BIOLOGICAL CHEMISTRY | 2002年 / 383卷 / 10期
关键词：
chaperone; haptoglobin; hemoglobin-haptoglobin complex; molecular modeling; protein aggregation; tertiary structure;
D O I：
10.1515/BC.2002.187
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：
With respect to the mechanism of chaperone-like activity, we examined the behavior of haptoglobin under heat shock conditions. Secondary structure changes during heat treatment were followed by circular dichroism, Raman and infrared spectroscopy. A model of the haptoglobin tetramer, based on its sequence homology with serine proteases and the CCP modules, has been proposed. Sequence regions responsible for the chaperone-like activity were not fully identical with the region that takes part in formation of the hemoglobin-haptoglobin complex. We can postulate the presence of at least two different chaperone-binding sites on each haptoglobin heavy chain.
引用
收藏
页码：1667 / 1676
页数：10
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