3tc2

Publication Abstract from PubMed

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 beta-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified.

Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato.,Meulenbroek EM, Thomassen EA, Pouvreau L, Abrahams JP, Gruppen H, Pannu NS Acta Crystallogr D Biol Crystallogr. 2012 Jul;68(Pt 7):794-9. doi:, 10.1107/S090744491201222X. Epub 2012 Jun 15. PMID:22751664^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.