Membrane protein association by potential intrarnembrane charge pairs (original) (raw)
- Letter
- Published: 30 May 1991
Nature volume 351, pages 414–416 (1991)Cite this article
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Abstract
THE transmembrane domain of the α chain of the T-cell receptor is responsible both for its assembly with the CD3 δ chain1 and for rapid degradation of the unassembled chain within the endoplasmic reticulum2,3. The determinant for both assembly and degradation is located in a segment of eight residues containing two basic amino acids (Fig. 1). We show here that placement of a single basic residue in the transmembrane domain of the Tac antigen can induce interaction with the CD3 chain, through its transmembrane acidic residue. This interaction is most favoured when the interacting residues are located at the same level in the membrane. The ability to induce protein–protein interaction by placing charge pairs within transmembrane domains suggests an approach to producing artificial dimers.
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Authors and Affiliations
- Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development National Institutes of Health, Bethesda, Maryland, 20892, USA
Pierre Cosson, Scott P. Lankford, Juan S. Bonifacino & Richard D. Klausner
Authors
- Pierre Cosson
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Cosson, P., Lankford, S., Bonifacino, J. et al. Membrane protein association by potential intrarnembrane charge pairs.Nature 351, 414–416 (1991). https://doi.org/10.1038/351414a0
- Received: 17 January 1991
- Accepted: 18 March 1991
- Issue Date: 30 May 1991
- DOI: https://doi.org/10.1038/351414a0