27GY
Juvenile hormone binding protein complexed with 2-Methyl-1-(4-propyloxybenzyl)-benzimidazole
This is a non-PDB format compatible entry.
Summary for 27GY
| Entry DOI | 10.2210/pdb27gy/pdb |
| Descriptor | Hemolymph juvenile hormone binding protein, 2-methyl-1-[(4-propoxyphenyl)methyl]benzimidazole, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | complex, transport protein |
| Biological source | Bombyx mori (domestic silkworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 25437.88 |
| Authors | Fujimoto, Z.,Tsuchiya, W.,Suzuki, R.,Shiotsuki, T. (deposition date: 2026-06-01, release date: 2026-07-15) |
| Primary citation | Gunasekara, U.K.D.S.S.,Inoue, K.,Fujimoto, Z.,Henmi, S.,Tsuchiya, W.,Suzuki, R.,Kutsuwada, K.,Ikeda, I.,Yamazaki, T.,Shiotsuki, T. Structural Characteristics for the Interaction of 1-Benzyl-2-Methylbenzimidazoles as Insect Growth Regulators and Juvenile Hormone Binding Protein. Insects, 17:-, 2026 Cited by PubMed Abstract: The authors previously reported that 2-methylbenzimidazole derivatives (MBIs) exhibit insect growth-regulating activity against the silkworm, . However, despite their unique effects on juvenile hormone (JH)-related endocrine pathways, the precise mode of action of MBIs remained unclear. In the present study, the interactions between MBIs and the lepidopteran hemolymph JH-binding protein (JHBP), a key regulator of JH transport and activity, were investigated using multiple approaches, including in vitro binding affinity assays, X-ray crystallography, and molecular docking simulations. A series of MBIs bearing a 1-(4-alkoxybenzyl) group, which exhibited potent insect growth-regulating activity, showed high binding affinity and structural compatibility with the JH-binding pocket of JHBP. In contrast, 1-(4-alkylbenzyl) MBIs, which displayed weak or negligible insect growth-regulating activity, exhibited low affinity for JHBP. These findings suggest that the insect growth-regulating activity of MBIs is mediated through inhibition of JHBP function, likely by disrupting the precise regulation of JH concentration in the hemolymph during larval development and pupal metamorphosis. PubMed: 42355390DOI: 10.3390/insects17060657 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.851 Å) |
Structure validation
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