Band 3 protein: Structure, flexibility and function
1994; Wiley; Volume: 346; Issue: 1 Linguagem: Inglês
10.1016/0014-5793(94)00468-4
ISSN1873-3468
Autores Tópico(s)Lipid Membrane Structure and Behavior
ResumoThe electroneutral exchange of chloride and bicarbonate across the human erythrocyte membrane is facilitated by Band 3, a 911 amino acid glycoprotein. The 43 kDa amino‐terminal cytosolic domain binds the cytoskeleton, haemoglobin and glycolytic enzymes. The 52 kDa carboxylterminal membrane domain mediates anion transport. The protein is a functional dimer, in which the two subunits probably interact with one another by an allosteric mechanism. It is proposed that the link between the mobile cytoplasmic and the membrane‐spanning domains of the protein is flexible, based on recent biochemical, biophysical and structural data. This explains the long‐standing puzzle that attachment to the cytoskeletal spectrin and actin does not appear to restrict the rotational movement of the Band 3 protein in the erythrocyte membrane. In the Band 3 isoform from the Southeast Asian Ovalocytes (SAO) this link is altered, resulting a tighter attachment of the cytoskeleton to the plasma membrane and a more rigid red blood cell.
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