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Molecules 2018, 23(1), 35; https://doi.org/10.3390/molecules23010035

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

Centre National de la Recherche Scientifique, Aix-Marseille Université, “Architecture et Fonction des Macromolécules Biologiques” Laboratory, 13288 Marseille, France
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Received: 5 December 2017 / Revised: 21 December 2017 / Accepted: 21 December 2017 / Published: 23 December 2017
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Abstract

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. View Full-Text
Keywords: α/β hydrolase fold; binding surface; cholinesterase-like domain; complex interface; crystal structure; four-helix bundle; dimer; tetramer; functional partnership α/β hydrolase fold; binding surface; cholinesterase-like domain; complex interface; crystal structure; four-helix bundle; dimer; tetramer; functional partnership
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Bourne, Y.; Marchot, P. Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains—A Structural Perspective. Molecules 2018, 23, 35.

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