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Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains—A Structural Perspective

机译:胆碱酯酶和相关的α/β水解酶折叠蛋白或结构域表面的蛋白质伙伴关系的热点—结构视角

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摘要

The hydrolytic enzymes acetyl- and butyryl-cholinesterase, the cell adhesion molecules neuroligins, and the hormonogenic macromolecule thyroglobulin are a few of the many members of the α/β hydrolase fold superfamily of proteins. Despite their distinctive functions, their canonical subunits, with a molecular surface area of ~20,000 Å2, they share binding patches and determinants for forming homodimers and for accommodating structural subunits or protein partners. Several of these surface regions of high functional relevance have been mapped through structural or mutational studies, while others have been proposed based on biochemical data or molecular docking studies. Here, we review these binding interfaces and emphasize their specificity versus potentially multifunctional character.
机译:水解酶乙酰胆碱酯酶和丁酰胆碱酯酶,细胞粘附分子神经胶蛋白和激素大分子甲状腺球蛋白是蛋白质的α/β水解酶折叠超家族中的少数成员。尽管它们具有独特的功能,但其典型的亚基具有约20,000Å 2 的分子表面积,它们共享结合斑块和决定簇,以形成同型二聚体并容纳结构性亚基或蛋白质伴侣。这些具有高功能相关性的表面区域中,有一些是通过结构或突变研究绘制的,而其他一些则是根据生化数据或分子对接研究提出的。在这里,我们回顾了这些绑定界面,并强调了它们的特异性与潜在的多功能特征。

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