Protein Structure and Modification of Aquaporins.
| Autor: | Xiong M; State Key Laboratory of Natural and Biomimetic Drugs, Department of Pharmacology, School of Basic Medical Sciences, Peking University, Beijing, China., Li C; Institute of Hypertension and Kidney Research, Zhongshan School of Medicine, Sun Yat-Sen University, Guangzhou, China., Wang W; Institute of Hypertension and Kidney Research, Zhongshan School of Medicine, Sun Yat-Sen University, Guangzhou, China. wangwd6@mail.sysu.edu.cn., Yang B; School of Basic Medical Sciences, Peking University, Beijing, China. baoxue@bjmu.edu.cn. |
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| Jazyk: | angličtina |
| Zdroj: | Advances in experimental medicine and biology [Adv Exp Med Biol] 2023; Vol. 1398, pp. 15-38. |
| DOI: | 10.1007/978-981-19-7415-1_2 |
| Abstrakt: | Aquaporins (AQPs) allow water molecules and other small, neutral solutes to quickly pass through membrane. The protein structures of AQPs solved by crystallographic methods or cryo-electron microscopy technology show that AQP monomer consists of six membrane-spanning alpha-helices that form the central water-transporting pore. AQP monomers assemble to form tetramers, forming the functional units in the membrane, to transport water or other small molecules. The biological functions of AQPs are regulated by posttranslational modifications, e.g., phosphorylation, ubiquitination, glycosylation, subcellular distribution, degradation and protein interactions. Modifications of AQP combined with structural properties contribute to a better functional mechanism of AQPs. Insight into the molecular mechanisms responsible for AQP modifications as well as gating and transport properties proved to be fundamental to the development of new therapeutic targets or reliable diagnostic and prognostic biomarkers. (© 2023. The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.) |
| Databáze: | MEDLINE |
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