Structure of the band 3 transmembrane domain.
Structure of the band 3 transmembrane domain.
复制标题
带 3 跨膜结构域的结构。
DOI：
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发表时间：
1996
影响因子：
1.6
通讯作者：
R. Reithmeier
中科院分区：
文献类型：
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作者：
J. W. Vince;R. Reithmeier
带3的N-糖基化膜结构域由多个跨膜片段组成，这些跨膜片段聚集在一起形成用于阴离子交换的受调节的跨膜通道。在这篇文章中，我们回顾了带3的膜结构域的结构特征。二维晶体的电子显微镜分析证实了蛋白质的二聚体性质，并提供了膜结构域的整体形状。跨膜片段中的高度序列同一性，以及发现这些片段是螺旋的并且在连接环的蛋白水解裂解后保持紧密结合，表明跨膜螺旋之间的相互作用是特异性的并且形成膜结构域的结构的基础。带3的N-糖基化对于蛋白质的转运功能不是必需的。N-糖基化诱变表明条带3可以在多个环上糖基化，并跨越膜12次。影响带3低聚糖结构和蛋白质其他特性的红细胞疾病（HEMPAS和SAO）是持续研究的主题。
The N-glycosylated membrane domain of band 3 consists of multiple membrane spanning segments that come together to form a regulated transmembrane passage for the exchange of anions. In this article we review the structural features of the membrane domain of band 3. Electron microscopic analysis of 2-dimensional crystals have confirmed the dimeric nature of the protein and has provided the overall shape of the membrane domain. The high degree of sequence identity in the transmembrane segments, and the finding that these segments are helical and remain tightly associated after proteolytic cleavage of the connecting loops, suggests that the interactions between transmembrane helices are specific and form the foundation for the structure of the membrane domain. N-glycosylation of band 3 is not essential for the transport function of the protein. N-glycosylation mutagenesis indicates that band 3 can be glycosylated on multiple loops and spans the membrane 12 times. Red cell diseases (HEMPAS and SAO) that affect the band 3 oligosaccharide structure and other properties of the protein are the subject of continued studies.