MRC OX-2 ANTIGEN - A LYMPHOID NEURONAL MEMBRANE GLYCOPROTEIN WITH A STRUCTURE LIKE A SINGLE IMMUNOGLOBULIN LIGHT CHAIN

MRC OX-2 ANTIGEN - A LYMPHOID NEURONAL MEMBRANE GLYCOPROTEIN WITH A STRUCTURE LIKE A SINGLE IMMUNOGLOBULIN LIGHT CHAIN
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DOI:
10.1002/j.1460-2075.1985.tb02324.x
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发表时间:
1985-01-01
期刊:
影响因子:
11.4
通讯作者:
BARCLAY, AN
BARCLAY, AN
中科院分区:
生物学1区
文献类型:
--
作者:
CLARK, MJ;GAGNON, J;BARCLAY, AN

文献摘要

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MRC OX-2抗原是在神经元、胸腺细胞、B细胞、滤泡树突细胞和内皮上发现的MW为41,000 - 47,000的大鼠细胞表面糖蛋白。据报道,该抗原的氨基酸序列是从使用寡核苷酸探针检测的c[互补]DNA克隆的核苷酸序列推断的。该序列含有248个氨基酸残基,其中202个残基可能在细胞外,具有2个与IG同源的结构域。N-末端结构域与IG V结构域和Thy-1抗原最匹配,而C-末端部分类似于IG C结构域。结构总体上类似于IG L链或T细胞受体β。链在每个MRC OX-2抗原结构域上鉴定了三个糖基化位点。
The MRC OX-2 antigen is a rat cell surface glycoprotein of MW 41,000-47,000 found on neurons, thymocytes, B cells, follicular dendritic cells and endothelium. The amino sequence for this antigen is reported as deduced from the nucleotide sequence of c[complementary]DNA clones detected by use of an oligonucleotide probe. The sequence contains 248 amino acid residues of which 202 residues are likely to be outside the cell with 2 domains that show homology with Ig. The N-terminal domain fits best with Ig V domains and Thy-1 antigen while the C-terminal part is like an Ig C domain. The structure overall is similar to an Ig L chain or the T cell receptor .beta. chain. Three glycosylation sites are identified on each of the MRC OX-2 antigen domains.