1C3Y
THP12-CARRIER PROTEIN FROM YELLOW MEAL WORM
Summary for 1C3Y
Entry DOI | 10.2210/pdb1c3y/pdb |
Descriptor | THP12 CARRIER PROTEIN (1 entity in total) |
Functional Keywords | ef-hand, all-alpha, antifreeze protein |
Biological source | Tenebrio molitor (yellow mealworm) |
Total number of polymer chains | 1 |
Total formula weight | 12334.80 |
Authors | Soennichsen, F.D. (deposition date: 1999-07-10, release date: 1999-11-10, Last modification date: 2024-10-23) |
Primary citation | Rothemund, S.,Liou, Y.C.,Davies, P.L.,Krause, E.,Sonnichsen, F.D. A new class of hexahelical insect proteins revealed as putative carriers of small hydrophobic ligands. Structure Fold.Des., 7:1325-1332, 1999 Cited by PubMed Abstract: THP12 is an abundant and extraordinarily hydrophilic hemolymph protein from the mealworm Tenebrio molitor and belongs to a group of small insect proteins with four highly conserved cysteine residues. Despite their sequence homology to odorant-binding proteins and pheromone-binding proteins, the function of these proteins is unclear. PubMed: 10574794DOI: 10.1016/S0969-2126(00)80022-2 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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