ArticleProtein science : a publication of the Protein Society2003
NMR characterization of interleukin-2 in complexes with the IL-2Ralpha receptor component, and with low molecular weight compounds that inhibit the IL-2/IL-Ralpha interaction.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 49 citations in OpenAlex.
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- Bioactive recombinant human oncostatin M for NMR-based screening in drug discovery.Scientific reports · 2021Article
- Structure and Function of an Inflammatory Cytokine, Interleukin-2, Analyzed Using the Bioinformatic Approach.The protein journal · 2019Article
- Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins.Biomolecules · 2019Article
- Inhibiting IL-2 signaling and the regulatory T-cell pathway using computationally designed peptides.Investigational new drugs · 2019Article
- Modulation of Protein-Protein Interactions for the Development of Novel Therapeutics.Molecular therapy : the journal of the American Society of Gene Therapy · 2016Review
- Advances in targeting cell surface signalling molecules for immune modulation.Nature reviews. Drug discovery · 2013Review
- Comparing Conformational Ensembles Using the Kullback-Leibler Divergence Expansion.Journal of chemical theory and computation · 2012Article
- Neutralizing endogenous chemokines with small molecules. Principles and potential therapeutic applications.Pharmacology & therapeutics · 2010Review
- Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles.Journal of chemical theory and computation · 2009Article
- An integrative in silico approach for discovering candidates for drug-targetable protein-protein interactions in interactome data.BMC pharmacology · 2007Article
- Amino-acid type identification in 15N-HSQC spectra by combinatorial selective 15N-labelling.Journal of biomolecular NMR · 2006Article
- 1H, 15N, and 13C resonance assignments of human interleukin-2.Journal of biomolecular NMR · 2005Article
- NMR structure of a complex between MDM2 and a small molecule inhibitor.Journal of biomolecular NMR · 2004Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear magnetic resonance (NMR) methods were employed to study the interaction of the cytokine Interleukin-2 (IL-2) with the alpha-subunit of its receptor (IL-2Ralpha), and to help understand the behavior of small molecule inhibitors of this interaction. Heteronuclear (1)H-(15)N HSQC experiments were used to identify the interaction surface of (15)N-enriched Interleukin-2 ((15)N-IL-2) in complex with human IL-2Ralpha. In these experiments, chemical shift and line width changes in the heteronuclear single-quantum coherence (HSQC) spectra upon binding of (15)N-IL-2 enabled classification of NH atoms as either near to, or far from, the IL-2Ralpha interaction surface. These data were complemented by hydrogen/deuterium (H/D) exchange measurements, which illustrated enhanced protection of slowly-exchanging IL-2 NH protons near the site of interaction with IL-2Ralpha. The interaction surface defined by NMR compared well with the IL-2Ralpha binding site identified previously using mutagenesis of human and murine IL-2. Two low molecular weight inhibitors of the IL-2/IL-2Ralpha interaction were studied: one (a cyclic peptide derivative) was found to mimic a part of the cytokine and bind to IL-2Ralpha; the other (an acylphenylalanine derivative) was found to bind to IL-2. For the interaction between IL-2 and the acylphenylalanine, chemical shift perturbations of (15)N and (15)NH backbone resonances were tracked as a function of ligand concentration. The perturbation pattern observed for this complex revealed that the acylphenylalanine is a competitive inhibitor-it binds to the same site on IL-2 that interacts with IL-2Ralpha.
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