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2RCK

Crystal structure of juvenile hormone binding protein from Galleria mellonella hemolymph

Summary for 2RCK
Entry DOI10.2210/pdb2rck/pdb
DescriptorJuvenile hormone binding protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (5 entities in total)
Functional Keywordsgalleria mellonella, hemolymph, jhbp-fold, juvenile hormone, hormone binding protein
Biological sourceGalleria mellonella (greater wax moth)
Total number of polymer chains2
Total formula weight50841.49
Authors
Kolodziejczyk, R.,Bujacz, G.,Jakob, M.,Ozyhar, A.,Jaskolski, M.,Kochman, M. (deposition date: 2007-09-20, release date: 2008-03-04, Last modification date: 2024-10-16)
Primary citationKolodziejczyk, R.,Bujacz, G.,Jakob, M.,Ozyhar, A.,Jaskolski, M.,Kochman, M.
Insect Juvenile Hormone Binding Protein Shows Ancestral Fold Present in Human Lipid-Binding Proteins.
J.Mol.Biol., 377:870-881, 2008
Cited by
PubMed Abstract: Low molecular weight juvenile hormone binding proteins (JHBPs) are specific carriers of juvenile hormone (JH) in the hemolymph of butterflies and moths. As hormonal signal transmitters, these proteins exert a profound effect on insect development. The crystal structure of JHBP from Galleria mellonella shows an unusual fold consisting of a long alpha-helix wrapped in a highly curved antiparallel beta-sheet. JHBP structurally resembles the folding pattern found in tandem repeats in some mammalian lipid-binding proteins, with similar organization of one cavity and a disulfide bond between the long helix and the beta-sheet. JHBP reveals, therefore, an archetypal fold used by nature for hydrophobic ligand binding. The JHBP molecule possesses two hydrophobic cavities. Several lines of experimental evidence conclusively indicate that JHBP binds JH in only one cavity, close to the N- and C-termini, and that this binding induces a structural change. The second cavity, located at the opposite end of the molecule, could bind another ligand.
PubMed: 18291417
DOI: 10.1016/j.jmb.2008.01.026
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.44 Å)
Structure validation

243531

数据于2025-10-22公开中

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