Ligand-induced, receptor-mediated dimerization and activation of EGF receptor.
The EGF receptor mediates many cellular responses in normal biological processes and in pathological states. Recent structural studies reveal the molecular basis for ligand binding specificity and how ligand binding induces receptor dimerization. Receptor dimerization is mediated by receptor-receptor interactions in which a loop protruding from neighboring receptors mediates receptor dimerization and activation.
Schlessinger
Joseph
J
Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA. joseph.schlessinger@yale.edu
D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000737:chemistry; D019281:Dimerization; D066246:ErbB Receptors / Q000737:chemistry* / Q000378:metabolism*; D016023:Integrins / Q000737:chemistry; D007700:Kinetics; D008024:Ligands; D008954:Models, Biological; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D038981:Receptors, Collagen; D019030:Receptors, Vitronectin / Q000737:chemistry; D016415:Sequence Alignment; D015398:Signal Transduction
D016023:Integrins; D008024:Ligands; D038981:Receptors, Collagen; D019030:Receptors, Vitronectin; D003094:Collagen; D066246:ErbB Receptors