Integrin-ligand binding. Do integrins use a 'MIDAS touch' to grasp an Asp?
Integrins use divalent cations, held within a novel 'MIDAS' motif, for ligand binding. It is proposed that a missing coordination site for the cation is provided by a critical acidic residue in the ligand.
Bergelson
J M
JM
Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Hemler
M E
ME
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D016023:Integrins / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D016177:Macrophage-1 Antigen / Q000737:chemistry / Q000378:metabolism; D008274:Magnesium / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000502:physiology; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D019010:Vascular Cell Adhesion Molecule-1 / Q000737:chemistry / Q000378:metabolism
D016023:Integrins; D008024:Ligands; D016177:Macrophage-1 Antigen; D009842:Oligopeptides; D019010:Vascular Cell Adhesion Molecule-1; C047981:arginyl-glycyl-aspartic acid; D008274:Magnesium