Polygalacturonase-inhibiting protein interacts with pectin through a binding site formed by four clustered residues of arginine and lysine.

@article{Spadoni2006PolygalacturonaseinhibitingPI,
  title={Polygalacturonase-inhibiting protein interacts with pectin through a binding site formed by four clustered residues of arginine and lysine.},
  author={Sara Spadoni and Olga A Zabotina and Adele Di Matteo and J\orn Dalgaard Mikkelsen and Felice Cervone and Giulia De Lorenzo and Benedetta Mattei and Daniela Bellincampi},
  journal={Plant physiology},
  year={2006},
  volume={141 2},
  pages={557-64}
}
Polygalacturonase-inhibiting protein (PGIP) is a cell wall protein that inhibits fungal polygalacturonases (PGs) and retards the invasion of plant tissues by phytopathogenic fungi. Here, we report the interaction of two PGIP isoforms from Phaseolus vulgaris (PvPGIP1 and PvPGIP2) with both polygalacturonic acid and cell wall fractions containing uronic acids. We identify in the three-dimensional structure of PvPGIP2 a motif of four clustered arginine and lysine residues (R183, R206, K230, and… CONTINUE READING

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