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Publication Abstract from PubMed

Innate ability to detect pathogens is achieved by pattern recognition receptors (PRRs) which recognise non-self components such as beta1,3-glucan. beta1,3-Glucans form a triple-helical structure stabilised by inter-chain hydrogen bonds. beta1,3-Glucan recognition protein (betaGRP)/gram-negative bacteria-binding protein 3 (GNBP3), one of PPRs, binds to long, structured beta1,3-glucan to initiate innate immune response. However, binding details and how specificity is achieved in such receptors remain important outstanding issues. We solved the crystal structures of the N-terminal beta1,3-glucan recognition domain of betaGRP/GNBP3 (betaGRP-N) in complex with the beta1,3-linked glucose hexamer, laminarihexaose. In the crystals, three structured laminarihexaoses simultaneously interact through six glucose residues (two from each chain) with one betaGRP-N. The spatial arrangement of the laminarihexaoses bound to betaGRP-N is almost identical to that of a beta1,3-glucan triplex. Therefore, our crystallographic structures together with site-directed mutagenesis data provide a structural basis for the unique recognition by such receptors of the triple-helix structure of beta1,3-glucan.

Structural insights into recognition of triple-helical {beta}-glucan by insect fungal receptor.,Kanagawa M, Satoh T, Ikeda A, Adachi Y, Ohno N, Yamaguchi Y J Biol Chem. 2011 Jun 22. PMID:21697086^[1]

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