3AQX

Crystal structure of Bombyx mori beta-GRP/GNBP3 N-terminal domain with laminarihexaoses

Summary for 3AQX

• Entry DOI: 10.2210/pdb3aqx/pdb
• Related: 2KHA 2RQE 3AQY 3AQZ 3IE4
• Descriptor: Beta-1,3-glucan-binding protein, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, GLYCEROL, ... (4 entities in total)
• Functional Keywords: beta-sandwich, immune receptor, beta-1, 3-glucan, sugar binding protein
• Biological source: Bombyx mori (silk moth, silkworm)
• Cellular location: Secreted (By similarity): Q9NL89
• Total number of polymer chains: 2
• Total formula weight: 25704.20

Authors

Kanagawa, M.,Satoh, T.,Ikeda, A.,Adachi, Y.,Ohno, N.,Yamaguchi, Y. (deposition date: 2010-11-22, release date: 2011-06-22, Last modification date: 2023-11-01)

Primary citation

Kanagawa, M.,Satoh, T.,Ikeda, A.,Adachi, Y.,Ohno, N.,Yamaguchi, Y.
Structural insights into recognition of triple-helical beta-glucans by an insect fungal receptor
J.Biol.Chem., 286:29158-29165, 2011

PubMed Abstract: The innate ability to detect pathogens is achieved by pattern recognition receptors, which recognize non-self-components such as β1,3-glucan. β1,3-Glucans form a triple-helical structure stabilized by interchain hydrogen bonds. β1,3-Glucan recognition protein (βGRP)/gram-negative bacteria-binding protein 3 (GNBP3), one of the pattern recognition receptors, binds to long, structured β1,3-glucan to initiate innate immune response. However, binding details and how specificity is achieved in such receptors remain important unresolved issues. We solved the crystal structures of the N-terminal β1,3-glucan recognition domain of βGRP/GNBP3 (βGRP-N) in complex with the β1,3-linked glucose hexamer, laminarihexaose. In the crystals, three structured laminarihexaoses simultaneously interact through six glucose residues (two from each chain) with one βGRP-N. The spatial arrangement of the laminarihexaoses bound to βGRP-N is almost identical to that of a β1,3-glucan triple-helical structure. Therefore, our crystallographic structures together with site-directed mutagenesis data provide a structural basis for the unique recognition by such receptors of the triple-helical structure of β1,3-glucan.

PubMed: 21697086
DOI: 10.1074/jbc.M111.256701

Experimental method

X-RAY DIFFRACTION (2.05 Å)