Computer modelling of human alpha 1-antitrypsin reactive site loop behaviour under mild conditions.

H Kołoczek; G Jezierski; M Pasenkiewicz-Gierula

doi:10.18388/abp.1996_4478

Computer modelling of human alpha 1-antitrypsin reactive site loop behaviour under mild conditions.

H Kołoczek Department of Physical Biochemistry, Jagiellonian University, Cracow, Poland.;
G Jezierski
M Pasenkiewicz-Gierula

DOI: https://doi.org/10.18388/abp.1996_4478

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.

Published

1996-09-30

Issue

Vol. 43 No. 3 (1996)

Section

Articles

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