Published April 11, 1988 | Version v1
Journal article Metadata-only

Site directed mutants of human interleukin-1α: a 1H-NMR and receptor binding study

Creators

  • 1. Max-Planck-Institut fuer Biochemie, Muenchen (Germany, F.R.)
  • 2. Glaxo Inst. for Molecular Biology, Geneva (Switzerland)
  • 3. Ludwig Inst. for Cancer Research, Epalinges (Switzerland)

Description

Mutant human interleukin-1α 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. 14 refs.; 2 figs.; 1 table

Additional details

Publishing Information

Journal Title
FEBS Letters
Journal Volume
231
Journal Issue
1
Series
FEBS Lett.
Journal Page Range
135-138
ISSN
0014-5793
CODEN
FEBLA

INIS

Country of Publication
Netherlands
Country of Input or Organization
Netherlands
INIS RN
20029461
Subject category
S60: APPLIED LIFE SCIENCES;
Descriptors DEI
AFFINITY; MAN; MUTANTS; NMR SPECTRA; NUCLEAR MAGNETIC RESONANCE; PROTEINS; PROTONS; RECEPTORS
Descriptors DEC
ANIMALS; BARYONS; CATIONS; CHARGED PARTICLES; ELEMENTARY PARTICLES; FERMIONS; HADRONS; HYDROGEN IONS; HYDROGEN IONS 1 PLUS; IONS; MAGNETIC RESONANCE; MAMMALS; NUCLEONS; ORGANIC COMPOUNDS; PRIMATES; RESONANCE; SPECTRA; VERTEBRATES