Istvan Botos

TL;DR: To establish the molecular basis for ligand binding and signaling, the crystal structure of a complex between two mouse TLR3-ECDs and dsRNA is determined at 3.4 angstrom resolution.

TL;DR: The membrane-bound Toll-like receptors trigger innate immune responses after recognition of a wide variety of pathogen-derived compounds and the nature of the interactions of the TLR extracellular domains with their ligands varies markedly between TLR paralogs.

TL;DR: The TLR3-ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors, including insertions in the LRRs and 11 N-linked glycans.

TL;DR: Alignment of the P domain catalytic pocket with those of several Ser-Lys dyad peptide hydrolases provides a model of substrate binding, suggesting that polypeptides are oriented in the Lon active site to allow nucleophilic attack by the serine hydroxyl on the si-face of the peptide bond.

TL;DR: The crystal structures of recombinant CV-N complexed to Man-9 and a synthetic hexamannoside show unequivocally the binding geometry of high mannose sugars toCV-N, permitting a better understanding of carbohydrate binding to this potential new lead for the design of drugs against AIDS.