7BIA
Crystal structure of human GSTP1 bound to iberin
Summary for 7BIA
| Entry DOI | 10.2210/pdb7bia/pdb |
| Descriptor | Glutathione S-transferase P, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLUTATHIONE, ... (5 entities in total) |
| Functional Keywords | glutathione transferase, ligandin, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 47923.92 |
| Authors | Schwartz, M.,Neiers, F. (deposition date: 2021-01-12, release date: 2022-03-02, Last modification date: 2024-01-31) |
| Primary citation | Schwartz, M.,Brignot, H.,Feron, G.,Hummel, T.,Zhu, Y.,von Koskull, D.,Heydel, J.M.,Lirussi, F.,Canon, F.,Neiers, F. Role of human salivary enzymes in bitter taste perception. Food Chem, 386:132798-132798, 2022 Cited by PubMed Abstract: The molecules that elicit taste sensation are perceived by interacting with the taste receptors located in the taste buds. Enzymes involved in the detoxification processes are found in saliva as well as in type II cells, where taste receptors, including bitter taste receptors, are located. These enzymes are known to interact with a large panel of molecules. To explore a possible link between these enzymes and bitter taste perception, we demonstrate that salivary glutathione transferases (GSTA1 and GSTP1) can metabolize bitter molecules. To support these abilities, we solve three X-ray structures of these enzymes in complexes with isothiocyanates. Salivary GSTA1 and GSTP1 are expressed in a large panel of subjects. Additionally, GSTA1 levels in the saliva of people suffering from taste disorders are significantly lower than those in the saliva of the control group. PubMed: 35344726DOI: 10.1016/j.foodchem.2022.132798 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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