title: The glycine-rich loop of adenylate kinase forms a giant anion hole.
abstract: The conformation of the glycine-rich loop of adenylate kinase is described in detail. It forms a giant anion hole for a sulfate ion, which presumably mimicks a nucleotide phosphoryl group. This loop had been called flexible, because at pH values of 6 or below it is displaced in the crystal. In the region of this loop the adenylate kinases are probably homologous to the p21 proteins. Is is known that a mutation in this loop at residue 12 of p21 causes cell transformation and therefore cancer. Other potentially homologous proteins are indicated.
mesh_terms: D000263:Adenylate Kinase; D000595:Amino Acid Sequence; D001665:Binding Sites; D005998:Glycine; D007477:Ions; D008958:Models, Molecular; D009711:Nucleotides / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D010770:Phosphotransferases; D011487:Protein Conformation; D011518:Proto-Oncogene Proteins; D013431:Sulfates / Q000378:metabolism
chemical_list: D007477:Ions; D009711:Nucleotides; D010710:Phosphates; D011518:Proto-Oncogene Proteins; D013431:Sulfates; D010770:Phosphotransferases; D000263:Adenylate Kinase; D005998:Glycine