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  • Title: Computer modelling of human alpha 1-antitrypsin reactive site loop behaviour under mild conditions.
    Author: Kołoczek H, Jezierski G, Pasenkiewicz-Gierula M.
    Journal: Acta Biochim Pol; 1996; 43(3):467-74. PubMed ID: 8922028.
    Abstract:
    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.
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