Circularly permuted interleukin 4 retains proliferative and binding activity.

Abstract:

:In human interleukin 4(IL-4), the carboxyl and amino termini of the 129 amino acid hormone are close to each other and this region is believed to be important for binding to the IL-4 receptor (IL-4r). We constructed plasmids encoding circularly permuted IL-4 mutants with the peptide Gly-Gly-Asn-Gly-Gly (GGNGG) joining the carboxyl to the amino terminus and with new amino and carboxyl termini elsewhere. Mutant IL-4(38-37) is composed of IL-4 residues 38-129 GGNGG and 1-37. Mutant IL-4(105-104) is composed of IL-4 residues 105-129, GGNGG and 1-104. IL-4(38-37) and IL-4(105-104) were purified from E. coli to near homogeneity and retained 50-100% of the binding and proliferative activity of IL-4, and in addition retained the ability to upregulate CD23 on Burkitt's lymphoma cells. Circular dichroism studies indicated that the tertiary structures of both IL-4(38-37) and IL-4(105-104) were retained, with the former molecule most similar to native IL-4. We conclude that while both native termini of IL-4 may be near its binding site, neither is required to be free for optimum activity.

journal_name

Cytokine

journal_title

Cytokine

authors

Kreitman RJ,Puri RK,McPhie P,Pastan I

doi

10.1006/cyto.1995.0039

subject

Has Abstract

pub_date

1995-05-01 00:00:00

pages

311-8

issue

4

eissn

1043-4666

issn

1096-0023

pii

S1043-4666(85)70039-7

journal_volume

7

pub_type

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