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- W2289451473 abstract "AE1 (band 3) is a major erythrocyte membrane protein that mediates Cl−/HCO3− exchange. The exchanger plays an important role in erythrocyte transport of HCO3− derived from metabolically produced CO2. AE1 (~100 kDa) consists of an ~55 kDa membrane domain and a cytoplasmic domain. The membrane domain mediates the Cl−/HCO3− exchange activity, whereas the cytoplasmic domain functions as an anchoring site for other membrane-associated proteins. In the erythrocyte membrane, AE1 is predominantly a dimer. Currently, there is no 3D model of full-length AE1. In the present study, we have generated a model of AE1 using 3D reconstruction of negatively stained AE1 dimers purified under non-denaturing conditions. Based on the shaded-surface view of the three-dimensional model generated from these images, we preliminarily assigned the membrane (M) and cytoplasmic (C) domains. The membrane domain has a central pore that may be involved in ion transport. The model is shown in two views rotated by a 90-degree rotation. Also shown is a representative electron micrograph of negatively stained AE1 dimers (marked with black arrows) used for 3D reconstruction. This is the first 3D model of full-length native AE1 protein. Supported by NIH." @default.
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- W2289451473 date "2010-04-01" @default.
- W2289451473 modified "2023-09-23" @default.
- W2289451473 title "Electron microscopy and three‐dimensional (3D) reconstruction of full‐length anion exchanger 1 (AE1)" @default.
- W2289451473 doi "https://doi.org/10.1096/fasebj.24.1_supplement.1002.1" @default.
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