title: Structures of Ras superfamily effector complexes: What have we learnt in two decades?
abstract: The Ras superfamily small G proteins are master regulators of a diverse range of cellular processes and act via downstream effector molecules. The first structure of a small G protein-effector complex, that of Rap1A with c-Raf1, was published 20 years ago. Since then, the structures of more than 60 small G proteins in complex with their effectors have been published. These effectors utilize a diverse array of structural motifs to interact with the G protein fold, which we have divided into four structural classes: intermolecular β-sheets, helical pairs, other interactions, and pleckstrin homology (PH) domains. These classes and their representative structures are discussed and a contact analysis of the interactions is presented, which highlights the common effector-binding regions between and within the small G protein families.
authors.affiliation: Department of Biochemistry, University of Cambridge , Cambridge , UK.
authors.forename: Helen R
authors.initials: HR
authors.lastname: Mott
authors.forename: Darerca
authors.initials: D
authors.lastname: Owen
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D020559:Monomeric GTP-Binding Proteins / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D046912:Multiprotein Complexes / Q000737:chemistry / Q000235:genetics; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D015398:Signal Transduction; D018631:ras Proteins / Q000737:chemistry* / Q000145:classification / Q000235:genetics
chemical_list: D046912:Multiprotein Complexes; D020559:Monomeric GTP-Binding Proteins; D018631:ras Proteins
keywords: Arf; GTPase; Rab; Ran; Ras; Rho; small G protein