ArticleJournal of molecular biology2014
The cytoplasmic domain of the T-cell receptor zeta subunit does not form disordered dimers.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- SCHOOL of nature: ligand-independent immunomodulatory peptides.Drug discovery today · 2020Article
- Article
- Extreme Fuzziness: Direct Interactions between Two IDPs.Biomolecules · 2019Review
- The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer.International journal of molecular sciences · 2018Article
- Targeting Intramembrane Protein-Protein Interactions: Novel Therapeutic Strategy of Millions Years Old.Advances in protein chemistry and structural biology · 2018Review
- Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness.Cellular and molecular life sciences : CMLS · 2017Review
- Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment.Frontiers in molecular biosciences · 2016Review
- Quarterly intrinsic disorder digest (January-February-March, 2014).Intrinsically disordered proteins · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Intrinsically disordered regions in proteins play active roles in recognition, signaling and molecular sorting. They often undergo coupled folding and binding giving rise to largely ordered interfaces with their binding partners. The cytoplasmic region of the T-cell receptor zeta subunit (ζcyt) has been previously proposed to specifically dimerize in the absence of a disorder-to-order transition, suggesting an intriguing dimerization mechanism that may involve multiple transient interfaces. We show here using analytical ultracentrifugation, NMR, size-exclusion chromatography (SEC) and multi-angle light scattering that neither ζcyt nor the cytoplasmic region of CD3ε significantly populates a dimeric state but that they are mostly monomers in solution up to millimolar concentrations. They experience a salt- and concentration-dependent shift of their elution volume in SEC previously interpreted as dimerization. Our data show that ζcyt does not form a highly disordered protein complex and leaves open the question as to whether completely disordered dimers (or other oligomers) exist in nature.
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Registered trials
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