Site directed mutants of human interleukin-1 alpha : a super(1)H-NMR and receptor binding study

Site directed mutants of human interleukin-1 alpha : a super(1)H-NMR and receptor binding study

Mutant human interleukin-1 alpha proteins were constructed by oligonucleotide directed mutagenesis. Six different mutants were tested for receptor binding activity and showed no alteration with respect to the wild-type protein. Analysis of these mutants by nuclear magnetic resonance spectroscopy con...

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Veröffentlicht in:FEBS letters 1988-01, Vol.231 (1), p.135-138
Hauptverfasser: Gronenborn, A M, Wingfield, P T, McDonald, H R, Schmeissner, U, Clore, G M
Format: Artikel
Sprache:eng
Schlagworte:
interleukin 1
N.M.R
site-directed mutagenesis
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Zusammenfassung:Mutant human interleukin-1 alpha proteins were constructed by oligonucleotide directed mutagenesis. Six different mutants were tested for receptor binding activity and showed no alteration with respect to the wild-type protein. Analysis of these mutants by nuclear magnetic resonance spectroscopy confirmed the structural integrity of the mutant proteins and permitted the sequence specific assignment of the histidine and tryptophan residues.
ISSN:0014-5793