| Title | A Recombinant Human [alpha]_1-Antitrypsin Variant, M_malton, Undergoes a Spontaneous Conformational Conversion into a Latent Form |
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| Author | Chan-Hun Jung and Hana Im * |
| Address | Department of Molecular Biology, Sejong University, 98 Gunja-dong, Kwangjin-gu, Seoul 143-747, Korea |
| Bibliography | Journal of Microbiology, 41(4),335-339, 2003, |
| DOI | |
| Key Words | antitrypsin, conformational change, latent form, serine protease inhibitors |
| Abstract | Many genetic variants of [alpha]_1-antitrypsin have been associated with early onset emphysema and liver cirrhosis. However, the detailed structural basis of pathogenic [alpha]_1-antitrypsin molecules is rarely known. Here we found that a recombinant M_malton variant (Phe52-deleted) lost inhibitory activity by spontaneous conformational conversion into a more stable, inactive form under physiological conditions. Biochemical and spectroscopic data suggested that the variant converts into a reactive center loop-inserted conformation, resembling the latent form of plasminogen activator inhibitor-1. |
| Download PDF | 414-05.pdf |