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

B. J. Classon; A. F. Williams; A. C. Willis; B. Seed; I. Stamenkovic

doi:10.1084/jem.169.4.1497

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

B. J. Classon, A. F. Williams, A. C. Willis, B. Seed, I. Stamenkovic

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106 Scopus citations

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.

Original language	English
Pages (from-to)	1497-1502
Number of pages	6
Journal	Journal of Experimental Medicine
Volume	169
Issue number	4
DOIs	https://doi.org/10.1084/jem.169.4.1497
State	Published - 1989
Externally published	Yes

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title = "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.",

author = "Classon, \{B. J.\} and Williams, \{A. F.\} and Willis, \{A. C.\} and B. Seed and I. Stamenkovic",

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T1 - The primary structure of the human leukocyte antigen CD37, a species homologue of the rat MRC OX-44 antigen

AU - Classon, B. J.

AU - Williams, A. F.

AU - Willis, A. C.

AU - Seed, B.

AU - Stamenkovic, I.

PY - 1989

Y1 - 1989

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0024511256

U2 - 10.1084/jem.169.4.1497

DO - 10.1084/jem.169.4.1497

M3 - Article

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AN - SCOPUS:0024511256

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VL - 169

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EP - 1502

JO - Journal of Experimental Medicine

JF - Journal of Experimental Medicine

IS - 4

ER -

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

Abstract

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