Computer modelling of human alpha 1-antitrypsin reactive site loop behaviour under mild conditions
| ISSN: | 1734-154X 0001-527X |
|---|---|
| DOI: | 10.18388/abp.1996_4478 |
| Přístupová URL adresa: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e4700edec690079fb6009872bc05ca5 https://doi.org/10.18388/abp.1996_4478 |
| Rights: | OPEN |
| Přírůstkové číslo: | edsair.doi.dedup.....9e4700edec690079fb6009872bc05ca5 |
| Autor: | Grzegorz Jezierski, Henryk Kołoczek, Marta Pasenkiewicz-Gierula |
| Rok vydání: | 1996 |
| Předmět: |
Binding Sites
biology Protein Conformation Hydrogen bond Chemistry Point mutation Active site Alpha (ethology) Hydrogen Bonding Serpin General Biochemistry Genetics and Molecular Biology Protein structure alpha 1-Antitrypsin Biophysics biology.protein Humans Computer Simulation Salt bridge Binding site |
| Zdroj: | Acta Biochimica Polonica. 43:467-474 |
| ISSN: | 1734-154X 0001-527X |
| DOI: | 10.18388/abp.1996_4478 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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