Rethinking pseudokinases.
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.
Kannan
Natarajan
N
Department of Chemistry, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92014-6054, USA.
Taylor
Susan S
SS
D051528:Guanylate Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
C106868:CASK kinases; D051528:Guanylate Kinases