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-Structure paper
タイトル | Molecular basis for human aquaporin inhibition. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 121, Issue 7, Page e2319682121, Year 2024 |
掲載日 | 2024年2月13日 |
![]() | Peng 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 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.2 Å |
構造データ | EMDB-16510, PDB-8c9h: |
化合物 | ![]() ChemComp-T60: |
由来 |
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![]() | MEMBRANE PROTEIN / aquaglyceroporin / glycerol channel / dimer of tetramers / inhibitor |