Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3zeta disrupt its interaction with Raf-1 kinase.
Wang H, Zhang L, Liddington R, Fu H.
Wang H, et al. Among authors: zhang l.
J Biol Chem. 1998 Jun 26;273(26):16297-304. doi: 10.1074/jbc.273.26.16297.
J Biol Chem. 1998.
PMID: 9632690
Free article.
Consistently, mutations on the charged surface of the groove (Lys-49, Arg-56, and Arg-60) decrease the binding of 14-3-3zeta to the ligands tested (Zhang, L., Wang, H., Liu, D., Liddington, R., and Fu, H. (1997) J. Biol. Chem. 272, 13717-13724). ...
Consistently, mutations on the charged surface of the groove (Lys-49, Arg-56, and Arg-60) decrease the binding of 14-3-3zeta to the ligands …