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
Institution
Title
The primary structure of the human leukocyte antigen CD37, a species homologue of the rat MRC OX-44 antigen.
Journal
The Journal of experimental medicine
ISSN
0022-1007 (Print)
ISSN-L
0022-1007
Publication state
Published
Issued date
01/04/1989
Peer-reviewed
Oui
Volume
169
Number
4
Pages
1497-1502
Language
english
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
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, Tetraspanin 25, Tetraspanins
Pubmed
Web of science
Open Access
Yes
Create date
25/08/2010 14:58
Last modification date
09/08/2024 9:28
Usage data
