A structural study of the carboxyl terminal region of the human erythrocyte band 3 protein.
A structural study of the carboxyl terminal region of the human erythrocyte band 3 protein.
复制标题
人红细胞带 3 蛋白羧基末端区域的结构研究。
DOI：
10.1093/oxfordjournals.jbchem.a125006
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发表时间：
1995
影响因子：
2.7
通讯作者：
N. Hamasaki
中科院分区：
文献类型：
--
作者：
A. Mori;K. Okubo;D. Kang;N. Hamasaki
源自人红细胞带 3 蛋白羧基末端区域的两种肽被鉴定为可在胰蛋白酶消化时从细胞膜释放的片段。然而，这些肽 Asn-880-Lys-892 和 Ala-893-Val-911-COOH 对胰蛋白酶具有抗性，除非细胞膜经过高浓度 NaOH 处理。这表明羧基末端区域原位位于天然带 3 分子内。与带 3 蛋白的其他部分（例如 Gly-647-Arg-656、Ser-731-Lys-743 和 Tyr-818-Lys-826）的情况不同，用 4,4'-二异硫氰芪-2,2'-二磺酸 (DIDS) 预处理红细胞不会抑制羧基末端区域的释放，表明存在向外和向内的形式之间的羧基末端部分没有主要的结构差异。带3蛋白的羧基末端区域具有负电荷簇。在负电荷簇的中间，在水通道蛋白 CHIP 和葡萄糖转运蛋白 1 的羧基末端区域分别发现了共有序列 Val-Asp-X-X-X-Leu-Asp-Ala-Asp-Asp 和 Thr-Phe-Asp-Glu (TFDE)。 TFDE 序列存在于葡萄糖转运蛋白 1 的高度两亲性 11 个残基序列中，并且该两亲性序列已被认为可以促进多位膜蛋白（例如葡萄糖转运蛋白 1 和丝氨酸化学感受器）的正常膜插入。讨论了带 3 蛋白羧基末端区域的作用。
Two peptides derived from the carboxyl terminal region of the human erythrocyte band 3 protein were identified as fragments releasable from cell membranes on trypsin digestion. These peptides, Asn-880-Lys-892 and Ala-893-Val-911-COOH, however, were resistant to trypsin, unless the cell membranes had been treated with high concentrations of NaOH. This suggests that the carboxyl terminal region is located in situ within the native band 3 molecule. Unlike in the cases of other portions of the band 3 protein, such as Gly-647-Arg-656, Ser-731-Lys-743, and Tyr-818-Lys-826, the release of the carboxyl terminal region was not inhibited by pretreatment of erythrocytes with 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS), indicating that there is no major structural difference in the carboxyl terminal portion between the outward and inward facing forms. The carboxyl terminal region of the band 3 protein has a negative charge cluster. In the middle of the negative charge cluster, consensus sequences, Val-Asp-X-X-X-Leu-Asp-Ala-Asp-Asp and Thr-Phe-Asp-Glu (TFDE), were found in the carboxyl terminal regions of aquaporin CHIP and glucose transporter 1, respectively. The sequence, TFDE, exists in the highly amphipathic 11-residue sequence of glucose transporter 1, and this amphipathic sequence has been suggested to promote normal membrane insertion of polytopic membrane proteins such as glucose transporter 1 and serine chemoreceptor. The role of the carboxyl terminal region of the band 3 protein is discussed.