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

Henryk Kołoczek | Zendy; G Jezierski | Zendy; Marta PasenkiewiczGierula | Zendy

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

Author(s) -

Henryk Kołoczek,

G Jezierski,

Marta PasenkiewiczGierula

Publication year - 1996

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.1996_4478

Subject(s) - serpin , chemistry , salt bridge , alpha (finance) , active site , loop (graph theory) , binding site , biochemistry , biophysics , mutant , stereochemistry , enzyme , biology , medicine , construct validity , nursing , mathematics , combinatorics , patient satisfaction , gene

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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