title: Ras-effector interactions: after one decade.
abstract: Ras effectors have convergently developed a common subdomain in their otherwise unrelated protein body for their interaction with Ras. Structural analysis revealed that the mode of interaction is highly similar for all Ras effectors, but is completely different from that of effectors of other subfamilies of small GTPases. Whereas the molecular mechanism of effector activation is still elusive, detailed knowledge about the thermodynamics and dynamics of the interaction with Ras has accumulated.
authors.affiliation: Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany. christian.herrmann@mpi-dortmund.mpg.de
authors.forename: Christian
authors.initials: C
authors.lastname: Herrmann
mesh_terms: D001665:Binding Sites; D004789:Enzyme Activation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012680:Sensitivity and Specificity; D015398:Signal Transduction / Q000502:physiology; D018631:ras Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D018631:ras Proteins