Structural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III).
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Authors
Glotzbach, BernhardSchmelz, Stefan
Reinwarth, Michael
Christmann, Andreas
Heinz, Dirk W
Kolmar, Harald

Issue Date
2013-01
Metadata
Show full item recordAbstract
In recent decades, several canonical serine protease inhibitor families have been classified and characterized. In contrast to most trypsin inhibitors, those from garden four o'clock (Mirabilis jalapa) and spinach (Spinacia oleracea) do not share sequence similarity and have been proposed to form the new Mirabilis serine protease inhibitor family. These 30-40-amino-acid inhibitors possess a defined disulfide-bridge topology and belong to the cystine-knot miniproteins (knottins). To date, no atomic structure of this inhibitor family has been solved. Here, the first structure of S. oleracea trypsin inhibitor III (SOTI-III), in complex with bovine pancreatic trypsin, is reported. The inhibitor was synthesized by solid-phase peptide synthesis on a multi-milligram scale and was assayed to test its inhibitory activity and binding properties. The structure confirmed the proposed cystine-bridge topology. The structural features of SOTI-III suggest that it belongs to a new canonical serine protease inhibitor family with promising properties for use in protein-engineering and medical applications.Citation
Structural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III). 2013, 69 (Pt 1):114-20 Acta Crystallogr. D Biol. Crystallogr.Affiliation
Institute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Germany.PubMed ID
23275169Type
ArticleLanguage
enISSN
1399-0047ae974a485f413a2113503eed53cd6c53
10.1107/S0907444912043880
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