Molecular area involved in the in-vitro dimerization of the murine p55 IL-2 receptor.

Abstract:

: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.

journal_name

Cytokine

journal_title

Cytokine

authors

Lorenzo F,Jaulin C,Jankovic DL,Theze J

doi

10.1016/1043-4666(92)90066-z

keywords:

subject

Has Abstract

pub_date

1992-07-01 00:00:00

pages

264-8

issue

4

eissn

1043-4666

issn

1096-0023

pii

1043-4666(92)90066-Z

journal_volume

4

pub_type

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