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• W4284968617 abstract "Evolution turned aquaporins (AQPs) into the most efficient facilitators of passive water flow through cell membranes at no expense of solute discrimination. In spite of a plethora of solved AQP structures, many structural details remain hidden. Here, by combining extensive sequence- and structural-based analysis of a unique set of 20 non-redundant high-resolution structures and molecular dynamics simulations of four representatives, key aspects of AQP stability, gating, selectivity, pore geometry, and oligomerization, with a potential impact on channel functionality, are identified. The general view of AQPs possessing a continuous open water pore is challenged and it is depicted that AQPs' selectivity is not exclusively shaped by pore-lining residues but also by the relative arrangement of transmembrane helices. Moreover, this analysis reveals that hydrophobic interactions constitute the main determinant of protein thermal stability. Finally, a numbering scheme of the conserved AQP scaffold is established, facilitating direct comparison of, for example, disease-causing mutations and prediction of potential structural consequences. Additionally, the results pave the way for the design of optimized AQP water channels to be utilized in biotechnological applications." @default.
• W4284968617 created "2022-07-10" @default.
• W4284968617 creator A5000580086 @default.
• W4284968617 creator A5000946042 @default.
• W4284968617 creator A5004764117 @default.
• W4284968617 creator A5012110398 @default.
• W4284968617 creator A5041035239 @default.
• W4284968617 creator A5041992046 @default.
• W4284968617 creator A5055394316 @default.
• W4284968617 date "2022-07-08" @default.
• W4284968617 modified "2023-10-18" @default.
• W4284968617 title "The Hidden Intricacies of Aquaporins: Remarkable Details in a Common Structural Scaffold" @default.
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