The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
T Cell Receptor-MHC Class I Peptide Interactions: Affinity, Kinetics, and Specificity
Abstract
The critical discriminatory event in the activation of T lymphocytes bearing alpha beta T cell receptors (TCRs) is their interaction with a molecular complex consisting of a peptide bound to a major histocompatibility complex (MHC)-encoded class I or class II molecule on the surface of an antigen-presenting cell. The kinetics of binding were measured of a purified TCR to molecular complexes of a purified soluble analog of the murine MHC class I molecule H-2Ld (sH-2Ld) and a synthetic octamer peptide p2CL in a direct, real-time assay based on surface plasmon resonance. The kinetic dissociation rate of the MHC-peptide complex from the TCR was rapid (2.6 x 10(-2) second-1, corresponding to a half-time for dissociation of approximately 27 seconds), and the kinetic association rate was 2.1 x 10(5) M-1 second-1. The equilibrium constant for dissociation was approximately 10(-7) M. These values indicate that TCRs must interact with a multivalent array of MHC-peptide complexes to trigger T cell signaling.
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Phenotypic Analysis of Antigen-Specific T Lymphocytes
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CD80 (B7-1) Binds Both CD28 and CTLA-4 with a Low Affinity and Very Fast Kinetics
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Metadata
- Authors
- Fisher, R. J., & Fivash, M.
- Venue
- Science
- Published
- 1995-04-07
- Volume
- 268
- Issue
- 5207
- Pages
- 115-117
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1975807928
- Cited by
- 296
- References
- 29
- FWCI
- 17.88
- Type
- journal article
- Language
- en
- Open access
- closed
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