Identification of residues involved in binding of IL5 to betacom using betaIL3 and betacom chimeras.
In mice there are two forms of the beta chain used in the IL3 receptor system, betacom and betaIL3. betacom is used by the IL3, IL5 and GM-CSF receptors whereas betaIL3 is only used in the IL3 receptor. In this work an assay was developed to identify residues of beta1L3 that restrict IL5 activity. It was found that such residues reside within the 2nd CRM of the molecule. Furthermore, when residues in the betaIL3 B'-C' loop were replaced with betacom sequence a form of betaIL3 was produced that was able to respond to IL5. This region is also responsible for IL3 binding to betaIL3 in the absence of alpha chain. It is therefore an important structural motif of betacom and betaIL3 responsible for both ligand interaction and specificity.
Czabotar
P E
PE
Division of Molecular Immunology, School of Biomedical Sciences, Curtin University of Technology, Perth, WA, Australia. petercz@cyllene.uwa.edu.au
Holland
J
J
Sanderson
C J
CJ
D000595:Amino Acid Sequence; D000818:Animals; D007377:Interleukin-3 / Q000378:metabolism; D015848:Interleukin-5 / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D011485:Protein Binding; D016185:Receptors, Interleukin-3 / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013601:T-Lymphocytes / Q000378:metabolism
D007377:Interleukin-3; D015848:Interleukin-5; D016185:Receptors, Interleukin-3; D011993:Recombinant Fusion Proteins