[HTML][HTML] Conversion of interleukin-13 into a high affinity agonist by a single amino acid substitution
We created a novel mutated form of human interleukin-13 (IL-13) in which a positively
charged arginine (R) at position 112 was substituted to a negatively charged aspartic acid
(D). This mutant, termed IL-13R112D, was expressed in Escherichia coli and purified to near
homogeneity. IL-13R112D was found to be a potent IL-13 agonist with 5–10-fold improved
binding affinity to IL-13 receptors compared with wild-type IL-13 (wtIL-13). The conclusion of
IL-13 agonist activity was drawn on the basis of approximately 10-fold improved activity over …
charged arginine (R) at position 112 was substituted to a negatively charged aspartic acid
(D). This mutant, termed IL-13R112D, was expressed in Escherichia coli and purified to near
homogeneity. IL-13R112D was found to be a potent IL-13 agonist with 5–10-fold improved
binding affinity to IL-13 receptors compared with wild-type IL-13 (wtIL-13). The conclusion of
IL-13 agonist activity was drawn on the basis of approximately 10-fold improved activity over …