Molecular recognition analyzed by docking simulations: the aspartate receptor and isocitrate dehydrogenase from Escherichia coli.
Protein docking protocols are used for the prediction of both small molecule binding to DNA and protein macromolecules and of complexes between macromolecules. These protocols are becoming increasingly automated and powerful tools for computer-aided drug design. We review the basic methodologies and strategies used for analyzing molecular recognition by computer docking algorithms and discuss recent experiments in which (i) substrate and substrate analogues are docked to the active site of isocitrate dehydrogenase and (ii) maltose binding protein is docked to the extracellular domain of the receptor, which signals maltose chemotaxis.
Stoddard
B L
BL
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Koshland
D E
DE
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000378:metabolism*; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D006860:Hydrogen Bonding; D007521:Isocitrate Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017459:Receptors, Amino Acid / Q000737:chemistry / Q000378:metabolism*
D004268:DNA-Binding Proteins; D017459:Receptors, Amino Acid; C031959:aspartic acid receptor; D001224:Aspartic Acid; D004247:DNA; D007521:Isocitrate Dehydrogenase