7YJJ
Human Cytosolic 10-formyltetrahydrofolate dehydrogenase and Gossypol complex
Summary for 7YJJ
| Entry DOI | 10.2210/pdb7yjj/pdb |
| EMDB information | 33872 |
| Descriptor | Cytosolic 10-formyltetrahydrofolate dehydrogenase, Gossypol (2 entities in total) |
| Functional Keywords | cytosolic 10-formyltetrahydrofolate dehydrogenase, aldehyde dehydrogenase family 1 member l1, inhibitor, gossypol, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 218275.54 |
| Authors | Han, C.W.,Lee, H.N.,Jeong, M.S.,Jang, S.B. (deposition date: 2022-07-20, release date: 2023-07-26, Last modification date: 2024-08-07) |
| Primary citation | Han, C.W.,Lee, H.N.,Jeong, M.S.,Kim, H.Y.,Jang, S.B. Structural identification and comprehension of human ALDH1L1-Gossypol complex. Biochem.Biophys.Res.Commun., 726:150306-150306, 2024 Cited by PubMed Abstract: The folate metabolism enzyme ALDH1L1 catalyzed 10-formyltetrahydrofolate to tetrahydrofolate and CO. Non-small cell lung cancer cells (NSCLC) strongly express ALDH1L1. Gossypol binds to an allosteric site and disrupts the folate metabolism by preventing NADP binding. The Cryo-EM structures of tetrameric C-terminal aldehyde dehydrogenase human ALDH1L1 complex with gossypol were examined. Gossypol-bound ALDH1L1 interfered with NADP by shifting the allosteric site of the structural conformation, producing a closed-form NADP binding site. In addition, the inhibition activity of ALDH1L1 was targeted with gossypol in NSCLC. The gossypol treatment had anti-cancer effects on NSCLC by blocking NADPH and ATP production. These findings emphasize the structure characterizing ALDH1L1 with gossypol. PubMed: 38917634DOI: 10.1016/j.bbrc.2024.150306 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.31 Å) |
Structure validation
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