Study of Chaperone-Like Activity of Human Haptoglobin: Conformational Changes under Heat Shock Conditions and Localization of Interaction Sites
Study of Chaperone-Like Activity of Human Haptoglobin: Conformational Changes under Heat Shock Conditions and Localization of Interaction Sites
复制标题
人触珠蛋白类伴侣活性的研究：热激条件下的构象变化和相互作用位点的定位
DOI：
10.1515/bc.2002.187
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发表时间：
2002
影响因子：
3.5
通讯作者：
Zdenek Pavlícek
中科院分区：
文献类型：
--
作者：
R. Ettrich;Wolfgang Brandt;Vladimír Kopecký;V. Baumruk;K. Hofbauerová;Zdenek Pavlícek
摘要结合珠蛋白在热休克条件下的行为，探讨了分子伴侣样活性的机制。通过圆二色谱、拉曼光谱和红外光谱研究了热处理过程中二级结构的变化。结合珠蛋白四聚体的模型，基于其与丝氨酸蛋白酶和CCP模块的序列同源性，已被提出。负责伴侣样活性的序列区域与参与血红蛋白结合珠蛋白复合物形成的区域不完全相同。我们可以假定在每个触珠蛋白重链上至少存在两个不同的伴侣结合位点。
Abstract With respect to the mechanism of chaperonelike 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 chaperonelike activity were not fully identical with the region that takes part in formation of the hemoglobinhaptoglobin complex. We can postulate the presence of at least two different chaperonebinding sites on each haptoglobin heavy chain.
影响因子：
2.9
作者：
MANAVALAN, P;JOHNSON, WC
通讯作者：
JOHNSON, WC
影响因子：
2.9
作者：
COMPTON, LA;JOHNSON, WC
通讯作者：
JOHNSON, WC
DOI：
10.1073/pnas.89.21.10449
发表时间：
1992-11-01
影响因子：
11.1
作者：
HORWITZ, J
通讯作者：
HORWITZ, J