title: Ion-dipole interactions and their functions in proteins.
abstract: Ion-dipole interactions in biological macromolecules are formed between atomic or molecular ions and neutral protein dipolar groups through either hydrogen bond or coordination. Since their discovery 30 years ago, these interactions have proven to be a frequent occurrence in protein structures, appearing in everything from transporters and ion channels to enzyme active sites to protein-protein interfaces. However, their significance and roles in protein functions are largely underappreciated. We performed PDB data mining to identify a sampling of proteins that possess these interactions. In this review, we will define the ion-dipole interaction and discuss several prominent examples of their functional roles in nature.
authors: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, 77030.
authors: Katherine H
authors: KH
authors: Sippel
authors: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, 77030.
authors: Florante A
authors: FA
authors: Quiocho
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D006801:Humans; D007477:Ions / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D007477:Ions; D011506:Proteins
keywords: ABC transport receptors; AP180; IMP dehydrogenase; Ion-dipole interaction; SNARE; ion channel; phage tail proteins; serine protease