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TitleStructural identification and comprehension of human ALDH1L1-Gossypol complex.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 726, Page 150306, Year 2024
Publish dateSep 24, 2024
AuthorsChang Woo Han / Han Na Lee / Mi Suk Jeong / Hong Yeoul Kim / Se Bok Jang /
PubMed AbstractThe 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 ...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.
External linksBiochem Biophys Res Commun / PubMed:38917634
MethodsEM (single particle)
Resolution6.31 Å
Structure data

33872

7yjj

EMDB-33872, PDB-7yjj:
Human Cytosolic 10-formyltetrahydrofolate dehydrogenase and Gossypol complex
Method: EM (single particle) / Resolution: 6.31 Å

Chemicals

ChemComp-GO3:
Gossypol

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / Cytosolic 10-formyltetrahydrofolate dehydrogenase / Aldehyde dehydrogenase family 1 member L1 / inhibitor / Gossypol

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