Tighter ties that bind

A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity. See Article p.529 Engineering an interleukin-2 'superkine' Chris Garcia an...

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Bibliographic Details
Published in:Nature (London) 2012-04, Vol.484 (7395), p.463-464
Main Author: Boder, Eric T.
Format: Article
Language:English
Subjects:
631/45/535
631/553/1886
692/699/67
692/700/565
Cancer
Crystallography
Humanities and Social Sciences
Immune response
Immune system
Interleukins
multidisciplinary
Mutation
news-and-views
Physiological aspects
Proteins
Science
Structural analysis
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Summary:A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity. See Article p.529 Engineering an interleukin-2 'superkine' Chris Garcia and colleagues elucidate the molecular mechanism that underlies the sensitization of T cells to the immunostimulatory cytokine interleukin-2 (IL-2). They use this information to engineer a single-chain IL-2 superkine that functions independent of its α-receptor (IL-2Rα or CD25). This new superkine is more efficacious than IL-2 in inducing antitumour T-cell responses and has fewer toxic side effects.
ISSN:0028-0836
1476-4687
DOI:10.1038/484463a