Igarashi K, Kaneda M, Yamaji A, Saido T C, Kikkawa U, Ono Y, Inoue K, Umeda M
Department of Inflammation Research, Tokyo Metropolitan Institute of Medical Science, Rinshoken, Japan.
J Biol Chem. 1995 Dec 8;270(49):29075-8. doi: 10.1074/jbc.270.49.29075.
A monoclonal anti-idiotypic antibody, Id8F7, previously shown to bind to a phosphatidylserine (PS)-specific binding site on protein kinase C (PKC) has been used to identify a 12-amino acid consensus sequence shared by PKC and phosphatidylserine decarboxylase (PSD). The 14-amino acid synthetic peptide derived from the corresponding region of PSD (amino acids 351-364 of the enzyme from Chinese hamster ovary cells) bound effectively and specifically to PS, and that derived from rat PKC gamma (amino acids 227-240) bound weakly but specifically to PS. Analysis of binding of Id8F7 to various synthetic peptides revealed that the consensus sequence motif, FXFXLKXXXKXR, is responsible for the interaction with both Id8F7 and PS. The results suggest that the conserved amino acid residues represent a basic structural motif for the specific interaction with PS, and the corresponding regions of PKC and PSD form the PS-specific binding sites of these enzymes.
一种单克隆抗独特型抗体Id8F7，先前已证明其可与蛋白激酶C（PKC）上的磷脂酰丝氨酸（PS）特异性结合位点结合，现被用于鉴定PKC和磷脂酰丝氨酸脱羧酶（PSD）共有的一个12个氨基酸的共有序列。源自PSD相应区域（中国仓鼠卵巢细胞中该酶的氨基酸351 - 364）的14个氨基酸合成肽能有效且特异性地结合PS，而源自大鼠PKCγ（氨基酸227 - 240）的合成肽则与PS结合较弱但具有特异性。对Id8F7与各种合成肽结合情况的分析表明，共有序列基序FXFXLKXXXKXR负责与Id8F7和PS的相互作用。结果表明，保守的氨基酸残基代表了与PS特异性相互作用的基本结构基序，PKC和PSD的相应区域形成了这些酶的PS特异性结合位点。
