Kannan Natarajan, Taylor Susan S
Department of Chemistry, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92014-6054, USA.
Cell. 2008 Apr 18;133(2):204-5. doi: 10.1016/j.cell.2008.04.005.
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.
假激酶在激酶核心中缺乏一个或多个催化残基的保守性,因此通常被认为是催化无活性的。穆克吉等人(2008年)的新研究对这一假设提出了挑战。他们表明,CASK(钙/钙调蛋白激活的丝氨酸-苏氨酸激酶)的假激酶结构域采用了一种活性构象,并在体内表现出催化活性。