The interaction of BMP-7 and ActRII implicates a new mode of receptor assembly.
The recently described structure of bone morphogenetic protein 7 in complex with the extracellular domain of the activin type receptor II provides a new and important paradigm to add to the list of possible modes of receptor assembly. A new mode of a ligand-mediated cooperative receptor assembly without receptor-receptor contacts yields new and exciting insights into the molecular signal transduction mechanism in the transforming growth factor-beta superfamily.
Sebald
Walter
W
Department of Physiological Chemistry II, Biocenter, University of Wuerzburg, Am Hubland, D-97074, Wuerzburg, Germany. sebald@biozentrum.uni-wuerzberg.de
Mueller
Thomas D
TD
D030301:Activin Receptors, Type II / Q000378:metabolism*; D000818:Animals; D055419:Bone Morphogenetic Protein 7; D019485:Bone Morphogenetic Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D007700:Kinetics; D008024:Ligands; D008954:Models, Biological; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016212:Transforming Growth Factor beta / Q000378:metabolism
D055419:Bone Morphogenetic Protein 7; D019485:Bone Morphogenetic Proteins; D008024:Ligands; D016212:Transforming Growth Factor beta; D030301:Activin Receptors, Type II; C425585:activin receptor type II-A