Hamasaki N
Department of Clinical Chemistry and Laboratory Medicine, Faculty of Medicine, Kyushu University, Japan.
Nihon Rinsho. 1996 Mar;54(3):618-24.
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.
人类红细胞的主要整合膜蛋白——带3蛋白，是一种阴离子交换体。体内的氧气输送系统由带3蛋白进行适当调控。带3蛋白的分子量为95 kDa，由两个主要结构域组成。氨基末端的390个残基形成一个水溶性的高度细长结构域，作为膜骨架和其他细胞质蛋白结合的附着位点。该蛋白的其余部分是一个55 kDa的疏水性结构域，负责催化阴离子转运。这种蛋白的丰富性使其成为研究转运蛋白结构-功能关系的有用模型。在本章中，我们将综述阴离子交换体的生理功能以及带3蛋白活性位点的结构-功能关系。
