title: Rethinking pseudokinases.
abstract: Pseudokinases lack conservation of one or more of the catalytic residues in the kinase core and as a consequence are typically thought to be catalytically inactive. New work by Mukherjee et al. (2008) challenges this assumption. They show that the pseudokinase domain of CASK (Ca2+/calmodulin activated serine-threonine kinase) adopts an active conformation and displays catalytic activity in vivo.
authors.affiliation: Department of Chemistry, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92014-6054, USA.
authors.forename: Natarajan
authors.initials: N
authors.lastname: Kannan
authors.forename: Susan S
authors.initials: SS
authors.lastname: Taylor
mesh_terms: D051528:Guanylate Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
chemical_list: C106868:CASK kinases; D051528:Guanylate Kinases