C─H⋯O hydrogen bonds in kinase-inhibitor interfaces.

ABSTRACT: C─H⋯O hydrogen bonds constitute a unique class of cohesive interactions. Their properties are similar to those of canonical H-bonds, although their energy is significantly lower, typically in the 0.5-2.5 kcal/mol range. Polarised C─H groups, such as those adjacent to electronegative groups, or within aromatic moieties, are particularly strong donors. C─H⋯O bonds are ubiquitous in nucleic acids and in proteins, notably stabilizing the β-sheet secondary structure. They have also been observed in numerous protein-ligand interactions. Here, we analysed crystal structures, deposited in the Protein Data Bank, of complexes of FDA-approved protein kinase inhibitors with cognate kinases, to assess the possible role of C─H^inhibitor ⋯O^protein hydrogen bonds. The conserved hinge

SUBMITTER: Derewenda ZS 

PROVIDER: S-EPMC7641297 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature