title: C1, see them all.
abstract: Recent structural analysis of crystalline beta2-chimaerin shows the central protein kinase C-like, diacylglycerol (DAG)-binding C1 domain to be masked by its intramolecular interactions with the N-terminal SH2 and GAP domains, and linker regions. A mechanism of activation has been derived from modelling of a GAP-Rac GTPase complex--the auto-inhibitory constraints are released via membrane engagement, unmasking the C1 domain to enable DAG binding and subsequent GAP stimulation of Rac GTPase catalytic activity.
authors.affiliation: Department of Molecular Neuroscience, Institute of Neurology, University College London, 1 Wakefield Street, London WC1N 1PJ, UK.
authors.forename: Christine
authors.initials: C
authors.lastname: Hall
authors.forename: Louis
authors.initials: L
authors.lastname: Lim
authors.forename: Thomas
authors.initials: T
authors.lastname: Leung
mesh_terms: D000818:Animals; D004075:Diglycerides / Q000378:metabolism; D006801:Humans; D009363:Neoplasm Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D011487:Protein Conformation; D020744:rac GTP-Binding Proteins / Q000378:metabolism
chemical_list: D004075:Diglycerides; D009363:Neoplasm Proteins; C079844:beta-chimaerin; D020744:rac GTP-Binding Proteins