Structural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III).
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Heinz, Dirk W
MetadataShow full item record
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.
CitationStructural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III). 2013, 69 (Pt 1):114-20 Acta Crystallogr. D Biol. Crystallogr.
AffiliationInstitute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Germany.
The following license files are associated with this item:
- Trypsin inhibitors from the garden four o'clock (Mirabilis jalapa) and spinach (Spinacia oleracea) seeds: isolation, characterization and chemical synthesis.
- Authors: Kowalska J, Pszczoła K, Wilimowska-Pelc A, Lorenc-Kubis I, Zuziak E, Ługowski M, Łegowska A, Kwiatkowska A, Sleszyńska M, Lesner A, Walewska A, Zabłotna E, Rolka K, Wilusz T
- Issue date: 2007 Jun
- Kunitz-type trypsin inhibitor with high stability from Spinacia oleracea L. seeds.
- Authors: Kang Z, Jiang JH, Wang D, Liu K, Du LF
- Issue date: 2009 Jan
- [Prospects for the design of new therapeutically significant protease inhibitors based on knottins and sunflower seed trypsin inhibitor (SFTI 1)].
- Authors: Kuznetsova SS, Kolesanova EF, Talanova AV, Veselovsky AV
- Issue date: 2016 May
- Thermodynamic criterion for the conformation of P1 residues of substrates and of inhibitors in complexes with serine proteinases.
- Authors: Qasim MA, Lu SM, Ding J, Bateman KS, James MN, Anderson S, Song J, Markley JL, Ganz PJ, Saunders CW, Laskowski M Jr
- Issue date: 1999 Jun 1
- Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition.
- Authors: Fodor K, Harmat V, Hetényi C, Kardos J, Antal J, Perczel A, Patthy A, Katona G, Gráf L
- Issue date: 2005 Jul 1