Key result
Six different mutant human interleukin-1 alpha proteins showed no alteration in receptor binding activity compared to the wild-type protein, with NMR confirming their structural integrity.
Site-directed mutagenesis of human IL-1 alpha did not alter receptor binding activity, and NMR permitted sequence-specific assignment of histidine and tryptophan residues.
May guide IL-1α engineering for research; leaves open translation to human cardiovascular applications.
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.
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Gronenborn et al. (1988) studied this question. Mutant human interleukin-1 alpha proteins vs. Wild-type protein was evaluated on Receptor binding activity and structural integrity. Six different mutant human interleukin-1 alpha proteins showed no alteration in receptor binding activity compared to the wild-type protein, with NMR confirming their structural integrity.
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