Kołoczek H, Jezierski G, Pasenkiewicz-Gierula M
Department of Physical Biochemistry, Jagiellonian University, Cracow, Poland.
Acta Biochim Pol. 1996;43(3):467-74.
Human alpha 1-antitrypsin (alpha 1-PI) is a member of the serpin superfamily of proteins. The reactive site loop (RSL) of the serpin binds to the active site of its target proteinase. Deficiency of alpha 1-antitrypsin is associated with a spontaneous conformational transition in the molecule which leads to a polymer formation. Mild conditions (1 M guanidinium.HCl), temperature and point mutations within the RSL are the factors that induce polymerisation. Initiation of this process has been associated with the disruption of a salt bridge Glu342-->Lys290. In this paper the interaction of guanidinium ion with Glu342 and Lys290 as well as the effect of this interaction on the mobility of RSL is studied by molecular modelling.
人α1-抗胰蛋白酶（α1-PI）是丝氨酸蛋白酶抑制剂超家族蛋白的成员。丝氨酸蛋白酶抑制剂的反应性位点环（RSL）与其靶蛋白酶的活性位点结合。α1-抗胰蛋白酶缺乏与分子中自发的构象转变有关，这种转变会导致聚合物形成。温和条件（1M盐酸胍）、温度和RSL内的点突变是诱导聚合的因素。该过程的起始与盐桥Glu342→Lys290的破坏有关。本文通过分子建模研究了胍离子与Glu342和Lys290的相互作用以及这种相互作用对RSL迁移率的影响。
