ArticleProtein science : a publication of the Protein Society1996
Kinetic analysis of ligand binding to interleukin-2 receptor complexes created on an optical biosensor surface.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
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- SHR-1916: A Novel PEGylated Interleukin-2 Analogue with Altered Cellular Selectivity and Improved Pharmacokinetic Profiles for Cancer Immunotherapy.Drug design, development and therapy · 2025Article
- A PD-1-targeted, receptor-masked IL-2 immunocytokine that engages IL-2Rα strengthens T cell-mediated anti-tumor therapies.Cell reports. Medicine · 2024Article
- Engineered cytokine/antibody fusion proteins improve IL-2 delivery to pro-inflammatory cells and promote antitumor activity.JCI insight · 2024Article
- Molecular reshaping of phage-displayed Interleukin-2 at beta chain receptor interface to obtain potent super-agonists with improved developability profiles.Communications biology · 2023Article
- Discriminating between negative cooperativity and ligand binding to independent sites using pre-equilibrium properties of binding curves.PLoS computational biology · 2020Article
- P15 peptide stimulates chondrogenic commitment and endochondral ossification.International orthopaedics · 2017Article
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- Identification of a gene for an ancient cytokine, interleukin 15-like, in mammals; interleukins 2 and 15 co-evolved with this third family member, all sharing binding motifs for IL-15Rα.Immunogenetics · 2014Article
- Cell-to-cell variability analysis dissects the plasticity of signaling of common γ chain cytokines in T cells.Science signaling · 2013Article
- Structural insights into the common γ-chain family of cytokines and receptors from the interleukin-7 pathway.Immunological reviews · 2012Review
- Simultaneous measurement of 10,000 protein-ligand affinity constants using microarray-based kinetic constant assays.Assay and drug development technologies · 2012Article
- Probing the binding mechanism and affinity of tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors.Protein science : a publication of the Protein Society · 2008Article
- Slow-dissociation effect of common signaling subunit beta c on IL5 and GM-CSF receptor assembly.Cytokine · 2008Article
- Solution assembly of the pseudo-high affinity and intermediate affinity interleukin-2 receptor complexes.Protein science : a publication of the Protein Society · 1999Article
- Interaction affinity between cytokine receptor components on the cell surface.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Extending the range of rate constants available from BIACORE: interpreting mass transport-influenced binding data.Biophysical journal · 1998Article
- Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
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Authors and funding
6 authors.
Funding
Abstract
The interleukin-2 receptor (IL-2R) is composed of at least three cell surface subunits, IL-2R alpha, IL-2R beta, and IL-2R gamma c. On activated T-cells, the alpha- and beta-subunits exist as a preformed heterodimer that simultaneously captures the IL-2 ligand as the initial event in formation of the signaling complex. We used BIAcore to compare the binding of IL-2 to biosensor surfaces containing either the alpha-subunit, the beta-subunit, or both subunits together. The receptor ectodomains were immobilized in an oriented fashion on the dextran matrix through unique solvent-exposed thiols. Equilibrium analysis of the binding data established IL-2 dissociation constants for the individual alpha- and beta-subunits of 37 and 480 nM, respectively. Surfaces with both subunits immobilized, however, contained a receptor site of much higher affinity, suggesting the ligand was bound in a ternary complex with the alpha- and beta-subunits, similar to that reported for the pseudo-high-affinity receptor on cells. Because the binding responses had the additional complexity of being mass transport limited, obtaining accurate estimates for the kinetic rate constants required global fitting of the data sets from multiple surface densities of the receptors. A detailed kinetic analysis indicated that the higher-affinity binding sites detected on surfaces containing both alpha- and beta-subunits resulted from capture of IL-2 by a preformed complex of these subunits. Therefore, the biosensor analysis closely mimicked the recognition properties reported for these subunits on the cell surface, providing a convenient and powerful tool to assess the structure-function relationships of this and other multiple subunit receptor systems.
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