+検索条件
-Structure paper
| タイトル | Altering the carbohydrate-binding specificity of the legume lectin FRIL through structure-guided engineering. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 17, Issue 1, Year 2026 |
| 掲載日 | 2026年3月5日 |
著者 | Yo-Min Liu / Hong Thuy Vy Nguyen / Xiaorui Chen / Md Shahed-Al-Mahmud / Ting-Hua Chen / Kuo-Shiang Liao / Jennifer M Lo / Tzu-Chun Kan / Chien-Tai Ren / Che Ma / ![]() |
| PubMed 要旨 | FRIL is a legume lectin from the hyacinth bean that has broad-spectrum antiviral activity. A distinctive trait of FRIL among similar mannose/glucose-specific legume lectins is that FRIL shows ...FRIL is a legume lectin from the hyacinth bean that has broad-spectrum antiviral activity. A distinctive trait of FRIL among similar mannose/glucose-specific legume lectins is that FRIL shows specificity for complex type N-glycans. We postulate that an extended binding site on FRIL facilitates this ligand selectivity. Here, we show legume lectin carbohydrate recognition domain (CRD) loop B is the main determinant of complex versus high-mannose N-glycan specificity in FRIL and Concanavalin A (ConA), respectively. First, we find that the inactive precursors of recombinant FRIL (rFRIL) and proConA (rproConA) can be activated via deglycosylation. Secondly, the cryo-EM structures of inactive apo rFRIL, active FRIL in complex with Galβ1,4-(Fucα1,3-)GlcNAcβ1,2-Man tetrasaccharide, and active rFRIL in complex with MannoseGlcNAc (Man9) N-glycan are determined, and residues H102 and Y101 on loop B are identified as crucial for complex glycan recognition. Finally, we swapped loop B residues 101 and 102 alongside loop C residue 145 on FRIL to their structural equivalent on ConA, resulting in a FRIL mutant that binds exclusively to high mannose N-glycans. Taken together, we have established a process of activating recombinant FRIL and related lectins through deglycosylation, and demonstrated the crucial role that loop B residues play in establishing oligosaccharide specificity. |
リンク | Nat Commun / PubMed:41786775 / PubMed Central |
| 手法 | EM (単粒子) / X線回折 |
| 解像度 | 2.4 - 2.67 Å |
| 構造データ | EMDB-64935, PDB-9vbx: EMDB-64936, PDB-9vby: EMDB-64937, PDB-9vbz: EMDB-64938, PDB-9vc0: ![]() PDB-9vbw: |
| 化合物 | ![]() ChemComp-CA: ![]() ChemComp-MN: ![]() ChemComp-HOH: |
| 由来 |
|
キーワード | PLANT PROTEIN / Flt3 receptor-interacting lectin / carbohydrate binding protein / lectin / glycoprotein / complex type glycan / FRIL / self glycan / high-mannose type glycan. OMS-FRIL |
ムービー
コントローラー
構造ビューア
万見文献について



著者

リンク











lablab purpureus (マメ科)
キーワード