title: The glycine-rich sequence of protein kinases: a multifunctional element.
abstract: Evolution favours the use of glycine-rich loops for nucleotide binding in proteins. In the large family of protein kinases, the catalytic domain of which has one of the highest degrees of conservation among all known proteins, the structure of the nucleotide-binding site differs from classical folds. We are now beginning to understand the multiple functional roles of the glycine-rich sequence in protein kinases and some of the structural constraints leading to its conservation.
authors.affiliation: German Cancer Research Centre, Department of Pathochemistry and Molecular Biology of Mitosis, Heidelberg, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Bossemeyer
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D005998:Glycine; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009711:Nucleotides / Q000378:metabolism; D011494:Protein Kinases / Q000737:chemistry*; D013379:Substrate Specificity
chemical_list: D009711:Nucleotides; D011494:Protein Kinases; D005998:Glycine