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.
MeSH Terms
Amino Acid Sequence
Animals
Antigens, Surface/genetics
Base Sequence
CD2 Antigens
Carrier Proteins/genetics
Cell Line
Cloning, Molecular
DNA/metabolism
Genes
Humans
RNA, Messenger/genetics
Receptors, Antigen, T-Cell/genetics
Receptors, Immunologic/genetics
T-Lymphocytes/immunology
Transcription, Genetic
Chemicals
Antigens, Surface
CD2 Antigens
Carrier Proteins
RNA, Messenger
Receptors, Antigen, T-Cell
Receptors, Immunologic
DNA
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Sayre P H
Chang H C
Hussey R E
Brown N R
Richardson N E
Spagnoli G
Clayton L K
Reinherz E L
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