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Titolo:
BIOLOGICAL AND RECEPTOR-BINDING ACTIVITIES OF HUMAN INTERLEUKIN-2 MUTATED AT RESIDUES 20ASP, 125CYS OR 127SER
Autore:
XU D; ECKENBERG R; MOREAU JL; LIU XY; THEZE J; BERTOGLIO J;
Indirizzi:
FAC PHARM PARIS 11,CJF INSERM 9301,5 RUE JEAN BAPTISTE CLEMENT F-92296 CHATENAY MALABRY FRANCE FAC PHARM PARIS 11,CJF INSERM 9301 F-92296 CHATENAY MALABRY FRANCE INST PASTEUR,UNITE IMMUNOGENET CELLULAIRE F-75015 PARIS FRANCE ACAD SINICA,SHANGHAI INST BIOCHEM SHANGHAI 200031 PEOPLES R CHINA
Titolo Testata:
European cytokine network
fascicolo: 4, volume: 6, anno: 1995,
pagine: 237 - 244
SICI:
1148-5493(1995)6:4<237:BARAOH>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOUSE INTERLEUKIN-2; IL-2 RECEPTOR; HIGH-AFFINITY; GAMMA-CHAIN; CELL LINES; BETA-CHAIN; IDENTIFICATION; ANTAGONIST; EXPRESSION; TRANSDUCTION;
Keywords:
INTERLEUKIN-2; AMINO-ACID SUBSTITUTION; BIOLOGICAL ACTIVITY; RECEPTOR BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
D. Xu et al., "BIOLOGICAL AND RECEPTOR-BINDING ACTIVITIES OF HUMAN INTERLEUKIN-2 MUTATED AT RESIDUES 20ASP, 125CYS OR 127SER", European cytokine network, 6(4), 1995, pp. 237-244

Abstract

We have used site-directed mutagenesis to analyse structure-function relationships of the human Interleukin-2 molecule, The mutations introduced targetted residue 20Asp, within the N-terminal A helix, as well as residues 125Cys and 127Ser in the C-terminal D helix. The results presented here demonstrate that destabilizing the C-terminus a helix through introduction of Pro residues in either positions 125 or 127 reduced the biological activity of IL-2 by a factor of 10 that was correlated with a decreased ability to bind the receptor, A number of substitutions in position 20 have an even more drastic effect on biological activity and receptor binding, However, specific substitutions such as 20Asn and 20Leu displayed a differential effect on human or mouse IL-2receptors. Furthermore, 2OLeu IL-2 was found to behave as a pal tial antagonist of natural IL-2 when tested on murine cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 18:52:03