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首页> 外文期刊>Journal of Molecular Biology >Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies.
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Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies.

机译：通过用N和C端区域特异性抗体修饰来确定HSP90二聚体中的单体排列。

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摘要

Electron microscopy using the low-angle rotary shadowing replica method showed that the HSP90 dimer consists of four globular domains aligning in a tandem fashion. When decorated with two monoclonal antibodies against epitopes mapped on the N-terminal region of HSP90, these antibodies bound to both ends of the HSP90 dimer. A C-terminal region specific antibody was shown to bind to the side of HSP90. These results support a model for HSP90 dimer whereby two HSP90 monomers are arranged in an antiparallel fashion and dimerize through the C-terminal domain. Treatment of HSP90 at elevated temperatures or with ATP at room temperature, though not with ADP, induces molecular transformation of the linear HSP90 dimer into an O-ring-shaped structure. Copyright 1999 Academic Press.
机译：使用低角度旋转阴影复制方法的电子显微镜显示，HSP90二聚体由四个球状结构域串联排列组成。当用针对定位在HSP90 N端区域的抗原决定簇的两种单克隆抗体修饰时，这些抗体结合到HSP90二聚体的两端。 C末端区域特异性抗体显示与HSP90侧结合。这些结果支持HSP90二聚体的模型，其中两个HSP90单体以反平行方式排列并通过C-末端结构域二聚。在高温下处理HSP90或在室温下用ATP处理（尽管不使用ADP处理）会诱导线性HSP90二聚体分子转化为O形环结构。版权所有1999，学术出版社。

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