Proteins from the PR-10 family are ubiquitously present in plants. They have similar three-dimensional structures but distinct properties.


Many PR-10 proteins are allergens. We determine their structures and study antibody binding, ligand binding, and covalent modifications.


As part of the plant's innate immune response, PR-10 proteins play a crucial role. They act by degrading th RNA of invading viruses and bacteria. 


We are currently investigating structural details of the ribonuclease activity experimentally, using mass spectrometry and NMR spectroscopy.


The PR-10 protein Pru p 1 binds single-stranded substrate RNA into the conserved binding pocket, priming it for endonucleolytic cleavage.

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