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Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3

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Citation

Wang, D. N., Sarabia, V. E., Reithmeier, R. A., & Kühlbrandt, W. (1994). Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3. EMBO Journal, 13(14), 3230-3235. doi:10.1002/j.1460-2075.1994.tb06624.x.


Cite as: http://hdl.handle.net/21.11116/0000-0007-DD94-9
Abstract
The electroneutral exchange of chloride and bicarbonate across the human erythrocyte membrane is facilitated by Band 3, a 911 amino acid glycoprotein consisting of a 43 kDa N-terminal cytosolic domain that binds the cytoskeleton, haemoglobin and glycolytic enzymes and a 52 kDa C-terminal membrane domain that mediates anion transport. Electron microscopy and three-dimensional image reconstruction of negatively stained two-dimensional crystals of the dimeric membrane domain revealed a U-shaped structure with dimensions of 60 x 110 A, and a thickness of 80 A. The structure is open on the top and at the sides, with the monomers in close contact at the base. The basal domain is 40 A thick and probably spans the lipid bilayer. The upper part of the dimer consists of two elongated protrusions measuring 25 x 80 A in projection, with a thickness of 40 A. The protrusions form the sides of a canyon, enclosing a wide space that narrows down and converges into a depression at the centre of the dimer on the top of the basal domain. This depression may represent the opening to a transport channel located at the dimer interface. Based on the available protein-chemical data, the two protrusions face the cytosolic side of the membrane and they appear to be dynamic.