[HTML][HTML] Alanine-scanning mutagenesis of α-helix D segment of interleukin-13 reveals new functionally important residues of the cytokine
AB Madhankumar, A Mintz, W Debinski - Journal of Biological Chemistry, 2002 - ASBMB
We documented that α-helices A, C, and D in human interleukin-13 (IL13) participate in
interaction with its respective receptors. We hypothesized that α-helix D is the site II of the
cytokine that binds IL13Rα1, a component of the normal tissue heterodimeric signaling
IL13/4 receptor (IL13/4R), and that α-helix D independently binds a monomeric IL13Rα2
receptor, which is a non-signaling glioma-restricted receptor for IL13. Therefore, we alanine-
scanned mutagenized helix D of IL13 to identify the residues involved in the respective …
interaction with its respective receptors. We hypothesized that α-helix D is the site II of the
cytokine that binds IL13Rα1, a component of the normal tissue heterodimeric signaling
IL13/4 receptor (IL13/4R), and that α-helix D independently binds a monomeric IL13Rα2
receptor, which is a non-signaling glioma-restricted receptor for IL13. Therefore, we alanine-
scanned mutagenized helix D of IL13 to identify the residues involved in the respective …