PH结构域是一种存在于多种信号转导蛋白和细胞骨架蛋白中的大约由120个氨基酸组成的功能性区域.不同蛋白质中的PH结构域在一级结构上的同源性并不很高,但其空间结构中肽链主链的折叠方式基本相同,而主要差别存在于其中的三个可变环上,含有这些环的侧面带有正电荷,被认为可能是其配体的结合部位.目前已知的配体有G蛋白βγ亚单位(Gβγ)、蛋白激酶C(PKC)和磷脂酰肌醇衍生物(PIP2或IP3),所以PH 结构域可能介导信号蛋白与这些分子间的相互作用,参与细胞信号转导网络的构成.
The PH domain is a protein module of approximately 120 amino acid residues founded in many proteins involved in signal transduction. The PH domains are similar to each other in their three-dimentional structures,and the major structure difference among them lies in the three variable loops in the structures. The PH domain is electrostatically-polarized and the variable loops are on the positively-charged surface, which may serve as a ligand-binding surface. So far ,it has been found that PH domains can interact with the βγ-subunits of G protein (Gβγ)、protein kinase C (PKC) and phosphatidylinositol-4,5-bisphosphate (PIP2 or inositol-1,4,5-trisphosphate (IP3)). All these implied that PH domain might play an important role in the interaction between the signaling molecules and help to form the signal transduction network.
王吉村,药立波. PH结构域的结构和功能研究进展[J].生物化学与生物物理进展,1998,25(3):245-249
复制生物化学与生物物理进展 ® 2025 版权所有 ICP:京ICP备05023138号-1 京公网安备 11010502031771号