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

• DOI: 10.1084/jem.166.4.923
• Publication Date: 2004-06-24T07:56:10Z
• Authors: B P Wallner; A Z Frey; R Tizard; R J Mattaliano; C Hession; M E Sanders; M L Dustin; T A Springer
• Keywords: Northern blot; Southern blot; Protein primary structure

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