Molecular area involved in the in-vitro dimerization of the murine p55 IL-2 receptor.
In order to study structure-function relationships of the M(r) 55,000 subunit of the murine IL-2R (p55 IL-2R) by epitope mapping, we have expressed the p55 IL-2R molecule in a cell-free translation system. Under these in vitro conditions, we detected the expected p55 IL-2R polypeptide initiated at Met 1 and, in addition, two internally initiated molecules at Met 64 and Met 105. In this report we describe that from such a mixture, containing three molecular species of p55 IL-2R, mAb 135D5 immunoprecipitated the polypeptide initiated at Met 105 although this N-terminally truncated form of p55 IL-2R does not contain its epitope located between amino acids 72-88. This observation can be taken as a further evidence for the formation of p55 IL-2R dimers. Finally, we identified the region implicated in the formation of p55 IL-2R dimers close to the transmembrane region of the molecule.
Lorenzo
F
F
Unité d'Immunogénétique Cellulaire, Institut Pasteur, Paris, France.
Jaulin
C
C
Jankovic
D L
DL
Theze
J
J
D000818:Animals; D000911:Antibodies, Monoclonal; D046911:Macromolecular Substances; D051379:Mice; D008970:Molecular Weight; D010446:Peptide Fragments; D011233:Precipitin Tests; D011487:Protein Conformation; D015375:Receptors, Interleukin-2 / Q000737:chemistry*; D011994:Recombinant Proteins
D000911:Antibodies, Monoclonal; D046911:Macromolecular Substances; D010446:Peptide Fragments; D015375:Receptors, Interleukin-2; D011994:Recombinant Proteins