Primary structure of lymphocyte function-associated antigen 3 (LFA-3). The ligand of the T lymphocyte CD2 glycoprotein.

Journal article

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.

Authors: Wallner, B; Frey, A; Tizard, R; Mattaliano, R; Hession, C

• Journal: Journal of experimental medicine
• Volume: 166
• Issue: 4
• Pages: 923-932
• Publication date: 1987-10-01
• DOI: 10.1084/jem.166.4.923
• EISSN: 1540-9538
• ISSN: 0022-1007
• Language: English
• Keywords: Molecular Sequence Data; Base Sequence; Cloning, Molecular; DNA; Humans; Antigens, Surface; Amino Acid Sequence; Antigens, Differentiation, T-Lymphocyte; Lymphocyte Function-Associated Antigen-1; Peptide Mapping