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MRC OX‐2 antigen: a lymphoid/neuronal membrane glycoprotein with a structure like a single immunoglobulin light chain.
Author(s) -
Clark M.J.,
Gag J.,
Williams A.F.,
Barclay A.N.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb02324.x
Subject(s) - biology , antigen , microbiology and biotechnology , immunoglobulin light chain , complementary dna , antibody , glycoprotein , peptide sequence , biochemistry , gene , genetics
The MRC OX‐2 antigen is a rat cell surface glycoprotein of mol. wt. 41 000‐47 000 found on neurones, thymocytes, B cells, follicular dendritic cells and endothelium. We now report the amino sequence for this antigen as deduced from the nucleotide sequence of cDNA 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 two domains that show homology with immunoglobulins. 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. Thus the structure overall is similar to an Ig light chain or the T cell receptor beta chain. Three glycosylation sites are identified on each of the MRC OX‐2 antigen domains.