Roles of ionic residues of the C1 domain in protein kinase C-α activation and the origin of phosphatidylserine specificity
On the basis of extensive structure-function studies of protein kinase C-α (PKC-α), we have
proposed an activation mechanism for conventional PKCs in which the C2 domain and the
C1 domain interact sequentially with membranes (Medkova, M., and Cho, W.(1999) J. Biol.
Chem. 274, 19852–19861). To further elucidate the interactions between the C1 and C2
domains during PKC activation and the origin of phosphatidylserine specificity, we mutated
several charged residues in two C1 domains (C1a and C1b) of PKC-α. We then measured …
proposed an activation mechanism for conventional PKCs in which the C2 domain and the
C1 domain interact sequentially with membranes (Medkova, M., and Cho, W.(1999) J. Biol.
Chem. 274, 19852–19861). To further elucidate the interactions between the C1 and C2
domains during PKC activation and the origin of phosphatidylserine specificity, we mutated
several charged residues in two C1 domains (C1a and C1b) of PKC-α. We then measured …
以上显示的是最相近的搜索结果。 查看全部搜索结果