Bostjan Kobe

TL;DR: New structural information has increased the understanding of the structural determinants of LRR proteins and the ability to model such proteins with unknown structures, and has shed new light on how these proteins participate in protein-protein interactions.

TL;DR: The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to beta-alpha structural units, which are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape.

TL;DR: It is shown that the flax rust fungus AvrL567 genes, whose products are recognized by the L5, L6, and L7 R proteins of flax, are highly diverse, with 12 sequence variants identified from six rust strains and suggested to represent an alternative outcome of plant-pathogen coevolution to indirect recognition associated with simple balanced polymorphisms for functional and nonfunctional R and Avr genes.

TL;DR: The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel β-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs.

TL;DR: This work has determined the crystal structure of the porcine inhibitor, which is the first three-dimensional structure of a protein containing leucine-rich repeats and represents a new class of α/β protein fold.