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- W2043041421 abstract "The residues located at the carboxyl terminus of helix D in interleukin-7 (IL-7) have previously been targeted as important for recruitment and binding to the gamma chain component of the IL-7 receptor (IL-7R). In this study, Trp 143 of helix D was mutated to His, Phe, Tyr and Pro and these mutants, along with a W143A mutant previously described, were studied to determine the effects on activation of DNA synthesis and binding affinity to IL-7R positive 2E8 cells. The W143F and W143Y mutants were similar to wild type IL-7 in their binding properties and retained 85% and 74% of their activating properties, respectively. In contrast, the W143H mutant possessed a lower binding affinity and a corresponding decrease in activation, the W143A mutant possessed an over 100-fold decreased binding affinity and some residual activation activity and the W143P mutant possessed a greatly decreased binding affinity and did not activate. These results strongly suggest an aromatic residue is required at position 143 for IL-7R binding and subsequent signal transduction." @default.
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- W2043041421 date "2002-03-01" @default.
- W2043041421 modified "2023-10-16" @default.
- W2043041421 title "STRUCTURE FUNCTION ANALYSIS OF INTERLEUKIN 7: REQUIREMENT FOR AN AROMATIC RING AT POSITION 143 OF HELIX D" @default.
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- W2043041421 doi "https://doi.org/10.1006/cyto.2002.1004" @default.
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