Structural and biologic properties of a human aspartic acid-126 interleukin-2 analog.

Abstract:

:Point mutations at position 141 in the murine interleukin-2 (IL-2) sequence have been reported to generate proteins with full antagonist activity on some IL-2-dependent cell lines. To evaluate the potential therapeutic utility of this observation, we have prepared recombinant human IL-2 with a point mutation at the corresponding position (Asp for Gln 126) and examined its structural and biologic properties. This mutation apparently induces minor changes in tertiary conformation accompanied by an increased sensitivity to changes in pH. The biologic activity of this analog is greatly reduced, primarily as a result of decreased affinity to the beta/gamma IL-2 receptor complex; however, it is only weakly antagonistic to the IL-2 response of normal peripheral blood lymphocytes.

journal_name

Arch Biochem Biophys

authors

Buchli P,Ciardelli T

doi

10.1006/abbi.1993.1608

subject

Has Abstract

pub_date

1993-12-01 00:00:00

pages

411-5

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(83)71608-5

journal_volume

307

pub_type

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