[Erythrocyte anion exchanger, band epsilon protein: structure and function].
The major integral membrane protein of human erythrocytes, the band 3 protein, is the anion exchanger. The oxygen delivering system in the body is properly controlled by the band 3 protein. The band 3 protein has a molecular mass of 95 kDa and consists of two major domains. The NH2-terminal 390 residues form a water-soluble, highly elongated domain that serves as an attachment site for the binding of the membrane skeleton and other cytoplasmic proteins. The remainder of the protein is a 55-kDa hydrophobic domain that is responsible for catalyzing anion transport. The abundance of this protein has made it a useful model for the study of structure-function relations in a transport protein. In this chapter, we review the physiological function of the anion exchanger and the structure-function relationship on the active site of the band 3 protein.
Department of Clinical Chemistry and Laboratory Medicine, Faculty of Medicine, Kyushu University, Japan.
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Hamasaki
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry / Q000502:physiology; D017920:Antiporters / Q000378:metabolism / Q000502:physiology; D001639:Bicarbonates / Q000378:metabolism; D001692:Biological Transport; D002713:Chlorine / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism; D006801:Humans
D001457:Anion Exchange Protein 1, Erythrocyte; D017920:Antiporters; D001639:Bicarbonates; D002713:Chlorine