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人Fc片段与金黄色葡萄球菌蛋白A的B片段形成的复合物的结晶、晶体结构分析及原子模型

Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus.

作者信息

Deisenhofer J, Jones T A, Huber R, Sjödahl J, Sjöquist J

出版信息

Hoppe Seylers Z Physiol Chem. 1978 Aug;359(8):975-85. doi: 10.1515/bchm2.1978.359.2.975.

Abstract

Crystals of the complex formed by human Fc fragment and fragment B (FB) of protein A from Staphylococcus aureus were prepared and the crystal structure determined at high resolution by multiple isomorphous replacement. Phase were improved considerably by combining these phases with calculated phases from the Fc component. FB is a small globular protein built of three parallel helices arranged in a triangular array. It binds by the first two helices of Fc and is attached to segments of CH2 and CH3. The CH3 module is unchanged between complex and Fc fragment crystals, but CH2 changes its position slightly relative to CH3. In addition, the upper third of CH2 is disordered in the complex crystals. Possible sources of this disorder are discussed.

摘要

制备了人Fc片段与金黄色葡萄球菌蛋白A的B片段(FB)形成的复合物晶体,并通过多重同晶置换法在高分辨率下测定了晶体结构。通过将这些相位与Fc组分的计算相位相结合,相位得到了显著改善。FB是一种由三个平行螺旋以三角形阵列排列而成的小球形蛋白质。它通过Fc的前两个螺旋结合,并附着于CH2和CH3片段。在复合物晶体和Fc片段晶体之间,CH3模块没有变化,但CH2相对于CH3的位置略有改变。此外,CH2的上三分之一在复合物晶体中是无序的。讨论了这种无序的可能来源。

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