Ontology highlight
ABSTRACT:
SUBMITTER: Ball LJ
PROVIDER: S-EPMC314220 | biostudies-literature | 2000 Sep
REPOSITORIES: biostudies-literature
Ball L J LJ Kühne R R Hoffmann B B Häfner A A Schmieder P P Volkmer-Engert R R Hof M M Wahl M M Schneider-Mergener J J Walter U U Oschkinat H H Jarchau T T
The EMBO journal 20000901 18
The Ena-VASP family of proteins act as molecular adaptors linking the cytoskeletal system to signal transduction pathways. Their N-terminal EVH1 domains use groups of exposed aromatic residues to specifically recognize 'FPPPP' motifs found in the mammalian zyxin and vinculin proteins, and ActA protein of the intracellular bacterium Listeria monocytogenes. Here, evidence is provided that the affinities of these EVH1-peptide interactions are strongly dependent on the recognition of residues flanki ...[more]