磷酸基团在3',5'-环磷酸腺苷依赖性蛋白激酶磷酸肽产物结构中的作用。
The role of the phosphate group for the structure of phosphopeptide products of adenosine 3',5'-cyclic monophosphate-dependent protein kinase.
作者信息
Hider R C, Ragnarsson U, Zetterqvist O
出版信息
Biochem J. 1985 Jul 15;229(2):485-9. doi: 10.1042/bj2290485.
Abstract
By c.d. studies it is shown that liver-pyruvate-kinase-related peptide substrates of cyclic AMP-dependent protein kinase have a high tendency towards non-random structures in non-aqueous media. When phosphorylated, the conformation tendencies decrease. This structural change is explained in terms of the formation of strong intrapeptide phosphate-guanidinium salt links. It is proposed that similar events occur at the catalytic site of protein kinase and that such an interaction could facilitate the removal of the phosphorylated products.
摘要
通过圆二色性研究表明，环磷酸腺苷依赖性蛋白激酶的肝丙酮酸激酶相关肽底物在非水介质中具有形成非随机结构的强烈倾向。磷酸化后，构象倾向降低。这种结构变化可以用肽内强磷酸 - 胍盐键的形成来解释。有人提出，类似的事件发生在蛋白激酶的催化位点，并且这种相互作用可能有助于磷酸化产物的去除。
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