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Ab initio MO studies of interaction mechanisms of Protein Kinase C with cell membranes

机译:从头开始MO研究蛋白激酶C与细胞膜相互作用的机制

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摘要

Protein Kinase C (PKC) is a family of regulatory enzymes. It is considered that binding with phorbol ester which are PKC activators, increases affinity of PKC for the membranes and consequently induces its conformation change. Electrostatic interactions between PKC and the membrane is assumed to be important, and performed ab initio MO calculations of one domain of PKC consisting of 50 amino acids and its complex with the ester is performed to investigate how the electrostatic potential of PKC changes through docking with the substrate. From the calculation, it is shown that the electrostatic potential of PKC near the binding site is dramatically affected through the binding, suggesting attractive interactions with the cell membrane.
机译:蛋白激酶C(PKC)是一类调节酶。认为与作为PKC活化剂的佛波酯的结合增加了PKC对膜的亲和力,并因此诱导了其构象变化。 PKC和膜之间的静电相互作用被认为是重要的,并从头开始对由50个氨基酸组成的PKC的一个结构域及其与酯的复合物进行了MO的计算,以研究PKC的静电势如何通过与PCK的对接而改变基质。从计算结果表明,结合位点附近的PKC的静电势通过结合而受到显着影响,表明与细胞膜的吸引力相互作用。

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