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


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.

SUBMITTER: Classon BJ 

PROVIDER: S-EPMC2189247 | biostudies-other | 1989 Apr

REPOSITORIES: biostudies-other

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

Classon B J BJ   Williams A F AF   Willis A C AC   Seed B B   Stamenkovic I I  

The Journal of experimental medicine 19890401 4


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  ...[more]

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