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- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2012
- ISSN
- 1399-0047
- eISSN
- 1399-0047
- DOI
- 10.1107/S090744491201222X
- pmid
- 22751664
- Publisher site
- See Article on Publisher Site
Abstract
Potato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double‐headed Kunitz‐type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive‐site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric double‐headed Kunitz‐type serine protease inhibitor structure to be determined. PSPI has a β‐trefoil fold and, based on the structure, two reactive‐site loops bearing residues Phe75 and Lys95 were identified.
Journal
Acta Crystallographica Section D – Wiley
Published: Jul 1, 2012