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. 1987 May;84(9):2941–2945. doi: 10.1073/pnas.84.9.2941

Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes.

P H Sayre, H C Chang, R E Hussey, N R Brown, N E Richardson, G Spagnoli, L K Clayton, E L Reinherz
PMCID: PMC304776  PMID: 2883656

Abstract

The T11 (CD2) sheep-erythrocyte-binding protein is a T-cell surface molecule involved in activation of T lymphocytes and thymocytes, including those lacking the T3-Ti antigen-receptor complex. The primary structure of T11 was deduced from protein microsequencing and cDNA cloning. The mature human protein appears to be divided into three domains: a hydrophilic 185 amino acid external domain bearing only limited homology to the T-cell surface protein T4 and the immunoglobulin kappa light chain variable region, a 25 amino acid hydrophobic transmembrane segment, and a 126 amino acid cytoplasmic domain rich in prolines and basic residues. Transfection of cDNAs encoding either the 1.7- or the 1.3-kilobase T11 mRNA into COS-1 cells resulted in expression of surface T11 epitopes as well as sheep-erythrocyte-binding capacity. The predicted structure is consistent with the possibility that T11 functions in signal transduction.

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