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Human IFN gamma receptor cytoplasmic domain: expression and interaction with HuIFN gamma.

Abstract：

:To investigate the structural basis for human interferon gamma (huIFN gamma) binding to intracellular regions of the human IFN gamma receptor (huIFN gamma R), we have subcloned and expressed the huIFN gamma R free of fusion proteins in the yeast strain Pichia pastoris. HuIFN gamma bound to the cytoplasmic domain of the receptor via the IFN gamma C-terminus. Binding was inhibited by both human and mouse C-terminus peptides. N-terminus peptides failed to inhibit cytoplasmic binding. Thus, while extracellular receptor domain binding is species specific, binding to the cytoplasmic domain of the receptor is species non-specific. In solid-phase binding assays, IFN gamma had a Kd of 3.7 x 10(-8) M for the newly expressed cytoplasmic domain. Peptide competitions showed that IFN gamma bound to a receptor site corresponding to the membrane proximal residues 253-287, which is adjacent to the site of binding of the tyrosine kinase JAK2. The cytoplasmic binding affinity and binding site specificity suggest that the huIFN gamma R cytoplasmic domain can function independent of the extracellular domain to bind huIFN gamma and induce the biological activity previously associated with internalized huIFN gamma.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Green MM,Larkin J 3rd,Subramaniam PS,Szente BE,Johnson HM

doi

10.1006/bbrc.1998.8077

subject

Has Abstract

pub_date

1998-02-04 00:00:00

pages

170-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)98077-9

journal_volume

243

pub_type

杂志文章

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