Discovering protein-ligand chalcogen bonding in the protein data bank using endocyclic sulfur-containing heterocycles as ligand search subsets
Discovering protein-ligand chalcogen bonding in the protein data bank using endocyclic sulfur-containing heterocycles as ligand search subsets
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DOI：
10.1007/s00894-017-3452-3
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发表时间：
2017-10-01
影响因子：
2.2
通讯作者：
Mitchell, Miguel O.
中科院分区：
文献类型：
--
作者：
Mitchell, Miguel O.
The chalcogen bond, the noncovalent, electrostatic attraction between covalently bonded atoms in group 16 and Lewis bases, is present in protein-ligand interactions based on X-ray structures deposited in the Protein Data Bank (PDB). Discovering protein-ligand chalcogen bonding in the PDB employed a strategy that focused on searching the database for protein complexes of five-membered, heterocyclic ligands containing endocyclic sulfur with endo electron-withdrawing groups (isothiazoles; thiazoles; 1,2,3-, 1,2.4-, 1,2,5-, 1,3,4-thiadiazoles) and thiophenes with exo electron-withdrawing groups, e.g., 2-chloro, 2-bromo, 2-amino, 2-alkylthio. Out of 930 ligands investigated, 33 or 3.5% have protein-ligand S-O interactions of which 31 are chalcogen bonds and two appear to be S-HO hydrogen bonds. The bond angles for some of the chalcogen bonds found in the PDB are less than 90 degrees, and an electrostatic model is proposed to explain this phenomenon.
