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STRUCTURE FUNCTION ANALYSIS OF INTERLEUKIN 7: REQUIREMENT FOR AN AROMATIC RING AT POSITION 143 OF HELIX D
- Source :
-
Cytokine . Mar2002, Vol. 17 Issue 5, p227. 7p. - Publication Year :
- 2002
-
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 γ 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. [Copyright &y& Elsevier]
- Subjects :
- *INTERLEUKINS
*GENETIC mutation
*DNA synthesis
*PROTEIN binding
Subjects
Details
- Language :
- English
- ISSN :
- 10434666
- Volume :
- 17
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Cytokine
- Publication Type :
- Academic Journal
- Accession number :
- 11258715
- Full Text :
- https://doi.org/10.1006/cyto.2002.1004