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We have isolated the cDNA for human lymphocyte function-associated antigen 3 (LFA-3), the ligand of the T lymphocyte CD2 molecule. The identity of the clones was established by comparison of the deduced amino acid sequence to the LFA-3 NH2-terminal and tryptic peptide sequences. The cDNA defines a mature protein of 222 amino acids that structurally resembles typical membrane-anchored proteins. An extracellular domain with six N-linked glycosylation sites is followed by a hydrophobic putative transmembrane region and a short cytoplasmic domain. The mature glycoprotein is estimated to be 44-68% carbohydrate. Southern blots of human genomic DNA indicate that only one gene codes for human LFA-3. Northern blot analysis demonstrates that the LFA-3 mRNA of 1.3 kb is widely distributed in human tissues and cell lines.

Type

Journal article

Journal

J Exp Med

Publication Date

01/10/1987

Volume

166

Pages

923 - 932

Keywords

Amino Acid Sequence, Antigens, Differentiation, T-Lymphocyte, Antigens, Surface, Base Sequence, Cloning, Molecular, DNA, Humans, Lymphocyte Function-Associated Antigen-1, Molecular Sequence Data, Peptide Mapping