The primary structure of the human leukocyte antigen CD37, a species homologue of the rat MRC OX-44 antigen.

Details

Serval ID
serval:BIB_FECC094B160A
Type
Article: article from journal or magazin.
Collection
Publications
Title
The primary structure of the human leukocyte antigen CD37, a species homologue of the rat MRC OX-44 antigen.
Journal
Journal of Experimental Medicine
Author(s)
Classon B.J., Williams A.F., Willis A.C., Seed B., Stamenkovic I.
ISSN
0022-1007[print], 0022-1007[linking]
Publication state
Published
Issued date
1989
Volume
169
Number
4
Pages
1497-1502
Language
english
Notes
Publication types: Comparative Study ; Journal Article
Abstract
Comparison of NH2-terminal protein sequence from the rat OX-44 antigen with the sequence of the human CD37 antigen deduced from a cDNA clone shows that these antigens are species homologues. The CD37 sequence is 244 amino acids in length and lacks a conventional leader sequence. The molecule is likely to have an NH2-terminal cytoplasmic domain followed by three transmembrane sequences that lie within the first 110 amino acids. The rest of the molecule is hydrophillic and contains three sites for N-linked glycosylation.
Keywords
Amino Acid Sequence, Antigens, CD, Antigens, CD20, Antigens, Differentiation/genetics, Antigens, Differentiation, B-Lymphocyte, Antigens, Differentiation, T-Lymphocyte/genetics, Antigens, Neoplasm, Base Sequence, DNA/genetics, Glycoproteins/genetics, Glycoproteins/ultrastructure, Molecular Sequence Data, RNA, Messenger/genetics, Solubility
Pubmed
Create date
25/08/2010 14:58
Last modification date
20/08/2019 16:29
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