通过疏水簇分析推导得出的HSP60和HSP70家族伴侣分子之间的结构相似性。
Structural similarities between chaperone molecules of the HSP60 and HSP70 families deduced from hydrophobic cluster analysis.
作者信息
Callebaut I, Catelli M G, Portetelle D, Burny A, Baulieu E E, Mornon J P
机构信息
Département des Macromolécules Biologiques, CNRS URA09, Universités Paris VI-Paris, France.
出版信息
FEBS Lett. 1994 Apr 11;342(3):242-8. doi: 10.1016/0014-5793(94)80510-5.
In this study, the conservation of strong structural landmarks between all the members of two chaperone families (HSP60 and HSP70) was deduced from their sequences by hydrophobic cluster analysis. On this basis, we propose that the ATP-binding environment is maintained by a similar fold in both protein families. The observed similarities extend throughout the proteins, including both the ATPase domain and the C-terminal substrate-binding domain.
在本研究中，通过疏水簇分析从两个伴侣蛋白家族（热休克蛋白60和热休克蛋白70）所有成员的序列中推断出强结构标志物的保守性。在此基础上，我们提出两个蛋白家族中ATP结合环境由相似的折叠结构维持。观察到的相似性贯穿整个蛋白质，包括ATP酶结构域和C端底物结合结构域。
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