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• W2100694556 endingPage "434" @default.
• W2100694556 startingPage "429" @default.
• W2100694556 abstract "Efficient activation and regulation of the cellular immune response requires engagement of T cell accessory molecules as well as the antigen-specific T cell receptor. The lymphocyte function-associated antigen (LFA) 3 (CD58)/CD2 accessory pathway, one of the first discovered, has been extensively characterized in terms of structure and function of the CD2 molecule, which is present on all T lymphocytes and natural killer cells of the human immune system. The binding site of human CD2 for LFA-3 has been localized to two epitopes on one face of the first immunoglobulin (Ig)-like domain of this two-domain, Ig superfamily molecule. Human LFA-3 is genetically linked and is 21% identical in amino acid sequence to CD2, suggesting that this adhesive pair may have evolved from a single ancestral molecule. We have aligned the amino acid sequences of LFA-3 and CD2 and mutagenized selected amino acids in the first domain of LFA-3 that are analogous to those implicated in the binding site of CD2. The data show that K30 and K34, in the predicted C-C' loop, and D84, in the predicted F-G loop of LFA-3, are involved in binding to CD2, suggesting that two complementary sites on one face of the first domain of each molecule bind to each other." @default.
• W2100694556 created "2016-06-24" @default.
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• W2100694556 date "1995-01-01" @default.
• W2100694556 modified "2023-10-18" @default.
• W2100694556 title "Amino acid residues required for binding of lymphocyte function-associated antigen 3 (CD58) to its counter-receptor CD2." @default.
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• W2100694556 doi "https://doi.org/10.1084/jem.181.1.429" @default.
• W2100694556 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2191834" @default.
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