与HLA - DR相关的恒定链的mRNA完整序列揭示了一种具有异常跨膜极性的多肽。
The complete sequence of the mRNA for the HLA-DR-associated invariant chain reveals a polypeptide with an unusual transmembrane polarity.
作者信息
Strubin M, Mach B, Long E O
出版信息
EMBO J. 1984 Apr;3(4):869-72. doi: 10.1002/j.1460-2075.1984.tb01898.x.
Abstract
A non-polymorphic polypeptide is associated intracellularly with the alpha and beta chains of murine Ia antigens and of human HLA-DR antigens. The exact role and the structure of this invariant chain have not been determined so far. A cDNA clone encoding the 33 000 dalton human invariant chain has been isolated. The nucleotide sequence of a near full-length cDNA clone, together with the sequence of the 5' portion of the mRNA determined by primer-extension, are reported here. The protein structure deduced from that sequence shows an unusual feature: the presence of a hydrophobic transmembrane region near the NH2 terminus, and of two glycosylation sites near the middle, indicates that the invariant chain has a polarity of membrane insertion which is inverted relative to histocompatibility antigens and most transmembrane proteins.
摘要
一种非多态性多肽在细胞内与小鼠Ia抗原及人类HLA - DR抗原的α链和β链相关联。到目前为止，这种恒定链的确切作用和结构尚未确定。已分离出一个编码33000道尔顿人类恒定链的cDNA克隆。本文报道了一个接近全长的cDNA克隆的核苷酸序列，以及通过引物延伸法确定的mRNA 5'部分的序列。从该序列推导的蛋白质结构显示出一个不寻常的特征：靠近NH2末端存在一个疏水跨膜区域，靠近中间位置有两个糖基化位点，这表明恒定链具有与组织相容性抗原及大多数跨膜蛋白相反的膜插入极性。
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