Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains—A Structural Perspective - Archive ouverte HAL Access content directly
Journal Articles Molecules Year : 2018

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

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 Ų, 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.
Fichier principal
Vignette du fichier
molecules-23-00035.pdf (1.3 Mo) Télécharger le fichier
Origin Publisher files allowed on an open archive
Loading...

Dates and versions

hal-01802955 , version 1 (08-06-2018)

Identifiers

Cite

Yves Bourne, Pascale Marchot. 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 (1), ⟨10.3390/molecules23010035⟩. ⟨hal-01802955⟩
101 View
52 Download

Altmetric

Share

Gmail Mastodon Facebook X LinkedIn More