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The Erythrocyte Anion-Exchange Protein

Primary Structure Deduced from the cDNA Sequence and a Model for Its Arrangement within the Plasma Membrane

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New Insights into Cell and Membrane Transport Processes

Part of the book series: New Horizons in Therapeutics ((NHTH))

Overview

A full-length cDNA encoding the mouse erythrocyte anion-exchange protein band 3 has been isolated and sequenced. Homology between the amino acid sequence deduced from this cDNA and that of published fragments of human band 3 confirms its identity. A model of the topology of band 3 within the plasma membrane is proposed that is based on published biochemical data and the deduced amino acid sequence. Twelve hydrophobic and amphipathic regions in the anion-exchange domain are proposed to span the membrane as α-helices, resulting in both C and N termini in the interior of the cell. The possibility is considered that these transmembrane helices are organized to form two hydrophilic channels per band 3 monomer, which undergo conformational changes during the anion-exchange cycle.

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Author information

Authors and Affiliations

  1. Whitehead Institute for Biomedical Research, 02142, Cambridge, Massachusetts, USA

    Ron R. Kopito & Harvey F. Lodish

  2. Department of Biology, Massachusetts Institute of Technology, 02142, Cambridge, Massachusetts, USA

    Harvey F. Lodish

Authors
  1. Ron R. Kopito
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  2. Harvey F. Lodish
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Editors and Affiliations

  1. Smith Kline & French Laboratories, Philadelphia, Pennsylvania, USA

    George Poste  & Stanley T. Crooke  & 

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© 1986 Plenum Press, New York

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Kopito, R.R., Lodish, H.F. (1986). The Erythrocyte Anion-Exchange Protein. In: Poste, G., Crooke, S.T. (eds) New Insights into Cell and Membrane Transport Processes. New Horizons in Therapeutics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5062-0_3

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  • DOI: https://doi.org/10.1007/978-1-4684-5062-0_3

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5064-4

  • Online ISBN: 978-1-4684-5062-0

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