3AQX
Crystal structure of Bombyx mori beta-GRP/GNBP3 N-terminal domain with laminarihexaoses
3AQX の概要
エントリーDOI | 10.2210/pdb3aqx/pdb |
関連するPDBエントリー | 2KHA 2RQE 3AQY 3AQZ 3IE4 |
分子名称 | 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) |
機能のキーワード | beta-sandwich, immune receptor, beta-1, 3-glucan, sugar binding protein |
由来する生物種 | Bombyx mori (silk moth, silkworm) |
細胞内の位置 | Secreted (By similarity): Q9NL89 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 25704.20 |
構造登録者 | Kanagawa, M.,Satoh, T.,Ikeda, A.,Adachi, Y.,Ohno, N.,Yamaguchi, Y. (登録日: 2010-11-22, 公開日: 2011-06-22, 最終更新日: 2023-11-01) |
主引用文献 | 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 Cited by 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: 21697086DOI: 10.1074/jbc.M111.256701 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.05 Å) |
構造検証レポート
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