The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains
The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains
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DOI：
10.1016/s0014-5793(03)01490-x
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发表时间：
2004-01-30
期刊：
影响因子：
3.5
通讯作者：
Oschkinat, H
中科院分区：
文献类型：
--
作者：
Brockmann, C;Leitner, D;Oschkinat, H
通过核磁共振光谱法测定了SODD BAG结构域的N-末端扩展构建体的溶液结构。SODD-BAG/HSP 70复合物的同源性模型揭示了额外的可能的相互作用，这些相互作用对BAG结构域的SODD亚家族是特异性的，而复合物的整体几何形状保持不变。弛豫速率测量表明，SODD的氨基酸N358-S375，这是以前分配给它的BAG结构域中没有结构化在我们的构建体。因此，SODD BAG结构域确实小于Bag 1中的同源结构域，从而定义了BAG结构域的新亚家族。(C)2004年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
The solution structure of an N-terminally extended construct of the SODD BAG domain was determined by nuclear magnetic resonance spectroscopy. A homology model of the SODD-BAG/HSP70 complex reveals additional possible interactions that are specific for the SODD subfamily of BAG domains while the overall geometry of the complex remains the same. Relaxation rate measurements show that amino acids N358-S375 of SODD which were previously assigned to its BAG domain are not structured in our construct. The SODD BAG domain is thus indeed smaller than the homologous domain in Bag1 defining a new subfamily of BAG domains. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.