- Abstract:
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The αβ T-cell coreceptor CD4 enhances immune responses more than 1 million-fold in some assays, and yet the affinity of CD4 for its ligand, peptide-major histocompatibility class II (pMHC II) on antigen-presenting cells, is so weak that it was previously unquantifiable. Here, we report that a soluble form of CD4 failed to bind detectably to pMHC II in surface plasmon resonance-based assays, establishing a new upper limit for the solution affinity at 2.5 mM. However, when presented multival...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted Manuscript
- Files:
-
-
(pdf, 1.6MB)
-
- Publisher copy:
- 10.1073/pnas.1513918113
-
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- Publisher:
- National Academy of Sciences Publisher's website
- Journal:
- Proceedings of the National Academy of Sciences Journal website
- Volume:
- 113
- Issue:
- 20
- Pages:
- 5682–5687
- Publication date:
- 2016-01-01
- DOI:
- EISSN:
-
1091-6490
- URN:
-
uuid:63b63256-b8dc-4001-a7c1-bad76e50d316
- Source identifiers:
-
615384
- Local pid:
- pubs:615384
- Paper number:
- 20
- Copyright holder:
- Jönsson et al.
- Copyright date:
- 2016
- Notes:
-
This is the accepted manuscript version of the article. The final version is available online from National Academy of Sciences at: https://doi.org/10.1073/pnas.1513918113
Journal article
Remarkably low affinity of CD4/peptide-major histocompatibility complex class II protein interactions
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