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TitleMolecular basis for human aquaporin inhibition.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 7, Page e2319682121, Year 2024
Publish dateFeb 13, 2024
AuthorsPeng Huang / Hannah Åbacka / Carter J Wilson / Malene Lykke Wind / Michael Rűtzler / Anna Hagström-Andersson / Pontus Gourdon / Bert L de Groot / Raminta Venskutonytė / Karin Lindkvist-Petersson /
PubMed AbstractCancer invasion and metastasis are known to be potentiated by the expression of aquaporins (AQPs). Likewise, the expression levels of AQPs have been shown to be prognostic for survival in patients ...Cancer invasion and metastasis are known to be potentiated by the expression of aquaporins (AQPs). Likewise, the expression levels of AQPs have been shown to be prognostic for survival in patients and have a role in tumor growth, edema, angiogenesis, and tumor cell migration. Thus, AQPs are key players in cancer biology and potential targets for drug development. Here, we present the single-particle cryo-EM structure of human AQP7 at 3.2-Å resolution in complex with the specific inhibitor compound Z433927330. The structure in combination with MD simulations shows that the inhibitor binds to the endofacial side of AQP7. In addition, cancer cells treated with Z433927330 show reduced proliferation. The data presented here serve as a framework for the development of AQP inhibitors.
External linksProc Natl Acad Sci U S A / PubMed:38319972 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

16510

8c9h

EMDB-16510, PDB-8c9h:
AQP7_inhibitor
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-T60:
ethyl 4-[(4-pyrazol-1-ylphenyl)methylcarbamoylamino]benzoate

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / aquaglyceroporin / glycerol channel / dimer of tetramers / inhibitor

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