Lazar Noureddine, Brakch Noureddine, Panchal Maï, Fahy Christine, Rholam Mohamed
Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, FRE 2621 CNRS, Université Paris6--Pierre et Marie Curie, 96 Boulevard Raspail, 75006 Paris, France.
Arch Biochem Biophys. 2007 Jul 15;463(2):231-6. doi: 10.1016/j.abb.2007.03.014. Epub 2007 Apr 5.
Statistical analysis of several potential dibasic cleavage sites reveals differences in the distribution of basic doublets when the in vivo cleaved sites were compared to those which are not cleaved. Analysis of the substrate specificity of protease Kex2 towards the pro-ocytocin/neurophysin processing domain (pro-OT/Np(7-15) with altered basic pairs shows a cleavage efficiency order in accord with the statistical data. Structural analysis of these substrates indicates that each basic pair is associated with a local and specific conformational change. Thus, the in vivo cleavage hierarchy of dibasic sites is encoded by both the nature of basic pairs and the plasticity of proteolytic processing domains.
对几个潜在的双碱性切割位点进行统计分析发现，将体内切割位点与未切割位点进行比较时，碱性双联体的分布存在差异。对蛋白酶Kex2针对催产素原/神经垂体素加工结构域（pro-OT/Np(7-15)，其碱性对发生改变）的底物特异性分析显示，切割效率顺序与统计数据一致。对这些底物的结构分析表明，每个碱性对都与局部特定的构象变化相关。因此，双碱性位点在体内的切割层次由碱性对的性质和蛋白水解加工结构域的可塑性共同编码。
