Band 3 protein: Structure, flexibility and function

FEBS Letters

Wang, Da Neng¹ 

[1] European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany

关键词: Band 3 protein;    Anion transporter;    Membrane protein structure;    Cytoskeleton;    Southeast Asian Ovalocytosis;   

DOI  :  10.1016/0014-5793(94)00468-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 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.

【 授权许可】

Unknown