2.50
Hdl Handle:
http://hdl.handle.net/10033/270795
Title:
Structural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III).
Authors:
Glotzbach, Bernhard; Schmelz, Stefan; Reinwarth, Michael; Christmann, Andreas; Heinz, Dirk W; Kolmar, Harald
Abstract:
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.
Affiliation:
Institute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Germany.
Citation:
Structural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III). 2013, 69 (Pt 1):114-20 Acta Crystallogr. D Biol. Crystallogr.
Journal:
Acta crystallographica. Section D, Biological crystallography
Issue Date:
Jan-2013
URI:
http://hdl.handle.net/10033/270795
DOI:
10.1107/S0907444912043880
PubMed ID:
23275169
Type:
Article
Language:
en
ISSN:
1399-0047
Appears in Collections:
Publications from Division of Molekulare Struktur Biologie (MOSB)

Full metadata record

DC FieldValue Language
dc.contributor.authorGlotzbach, Bernharden_GB
dc.contributor.authorSchmelz, Stefanen_GB
dc.contributor.authorReinwarth, Michaelen_GB
dc.contributor.authorChristmann, Andreasen_GB
dc.contributor.authorHeinz, Dirk Wen_GB
dc.contributor.authorKolmar, Haralden_GB
dc.date.accessioned2013-03-01T09:44:17Z-
dc.date.available2013-03-01T09:44:17Z-
dc.date.issued2013-01-
dc.identifier.citationStructural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III). 2013, 69 (Pt 1):114-20 Acta Crystallogr. D Biol. Crystallogr.en_GB
dc.identifier.issn1399-0047-
dc.identifier.pmid23275169-
dc.identifier.doi10.1107/S0907444912043880-
dc.identifier.urihttp://hdl.handle.net/10033/270795-
dc.description.abstractIn 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.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Acta crystallographica. Section D, Biological crystallographyen_GB
dc.titleStructural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III).en
dc.typeArticleen
dc.contributor.departmentInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Germany.en_GB
dc.identifier.journalActa crystallographica. Section D, Biological crystallographyen_GB

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