Stable isotope aided nuclear magnetic resonance study to investigate the receptor-binding site of human interleukin 1 beta.

doi:10.1021/bi00123a032

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Article

Stable isotope aided nuclear magnetic resonance study to investigate the receptor-binding site of human interleukin 1 beta.

Biochemistry - 3 Mar 1992

Tate S, Kikumoto Y, Ichikawa S, Kaneko M, Masui Y, Kamogashira T, Ouchi M, Takahashi S, Inagaki F

Abstract excerpt

Resonance assignments for interleukin 1 beta at neutral pH were made by using three-dimensional NMR in combination with specific labeling and double-labeling methods with stable isotopes. On the basis of the present assignments, 15N single-quantum coherence spectra of N-terminal truncated and fusion mutants were compared with that of the wild-type. Although these mutants have reduced biological activity, they...

Topics

Amides
Amino Acid Sequence
Animals
CHO Cells
Cricetinae
Humans
Hydrogen-Ion Concentration
Interleukin-1
Magnetic Resonance Spectroscopy
Mice
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nitrogen Isotopes

Protein Binding

Protein Conformation

Receptors, Immunologic

Receptors, Interleukin-1

Solutions

Source

Open in PubMed

Identifiers

PMID: 1531768
DOI: 10.1021/bi00123a032

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1531768-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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