Matsuo M, Huang C H, Huang L C
Biochem J. 1978 Aug 1;173(2):441-7. doi: 10.1042/bj1730441.
On the basis of the chemical and structural features of the amino acid sequences in the vicinities of phosphorylatable hydroxyamino acid residues in several of the well-known protein substrates for skeletal-muscle cyclic AMP-dependent protein kinase, it is hypothesized that the phosphorylatable residue at position i and arginine residue at position i-3 of these protein substrates are located on a peptide turn on the hydrophilic protein surface. It is further hypothesized that there is an arginine-recognition site near the active centre on the protein kinase. This site is essential for the function of cyclic AMP-dependent protein kinase, for, not only does it recognize specifically the exposed arginine residue of the protein substrate, but, more importantly, via the interaction with arginine-(i--3), it may help to steer the topologically adjacent serine-i into proper orientation on the nearby active centre for phosphorylation. Model-building and kinetic data that provide support for the proposed hypotheses are presented.
基于几种著名的骨骼肌环磷酸腺苷依赖性蛋白激酶的蛋白质底物中可磷酸化羟基氨基酸残基附近氨基酸序列的化学和结构特征,推测这些蛋白质底物中第i位的可磷酸化残基和第i - 3位的精氨酸残基位于亲水性蛋白质表面的肽转角上。进一步推测,蛋白激酶活性中心附近存在一个精氨酸识别位点。该位点对于环磷酸腺苷依赖性蛋白激酶的功能至关重要,因为它不仅能特异性识别蛋白质底物暴露的精氨酸残基,更重要的是,通过与精氨酸 - (i - 3) 的相互作用,它可能有助于将拓扑相邻的丝氨酸 - i引导至附近活性中心的适当方向进行磷酸化。本文给出了为所提出的假设提供支持的模型构建和动力学数据。