title: How often does the myristoylated N-terminal latch of c-Abl come off?
abstract: The myristoylated N-terminal latching to the C-terminal lobe of c-Abl was recently demonstrated to be an important regulatory element for the kinase, playing a role similar to that of the tyrosine-phosphorylated C-terminal tail of c-Src. A potential mechanism for activating c-Abl is the dissociation of the myristoylated N-terminal latch. How often does this latch spontaneously come off? A recent theoretical model along with the experimental results of Superti-Furga, Kuriyan, and co-workers suggests that the equilibrium fraction of c-Abl in which the myristoylated N-terminal is unlatched is approximately 0.5%.
authors.affiliation: Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA. zhou@sb.fsu.edu
authors.forename: Huan-Xiang
authors.initials: HX
authors.lastname: Zhou
mesh_terms: D004789:Enzyme Activation; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008958:Models, Molecular; D009227:Myristic Acids / Q000737:chemistry; D011487:Protein Conformation; D016315:Proto-Oncogene Proteins c-abl / Q000737:chemistry* / Q000378:metabolism
chemical_list: D009227:Myristic Acids; D016315:Proto-Oncogene Proteins c-abl