Membrane protein association by potential intramembrane charge pairs

The transmembrane domain of the alpha chain of the T-cell receptor is responsible both for its assembly with the CD3 delta chain and for rapid degradation of the unassembled chain within the endoplasmic reticulum. The determinant for both assembly and degradation is located in a segment of eight res...

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Bibliographic Details
Published in:Nature (London) 1991-05, Vol.351 (6325), p.414-416
Main Authors: COSSON, P, LANKFORD, S. P, BONIFACINO, J. S, KLAUSNER, R. D
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Antigens, Differentiation, T-Lymphocyte - chemistry
Biological and medical sciences
Biology
CD3 antigen
CD3 Complex
DNA Mutational Analysis
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Humans
Hydrogen Bonding
Immunobiology
In Vitro Techniques
Ions
Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation
Macromolecular Substances
Membrane Proteins - chemistry
Mice
Molecular Sequence Data
Protein Binding
Proteins
Receptors, Antigen, T-Cell - chemistry
Receptors, Antigen, T-Cell, alpha-beta
Receptors, Interleukin-2 - chemistry
Recombinant Fusion Proteins
Residues
Structure-Activity Relationship
T-cell receptor
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Summary:The transmembrane domain of the alpha chain of the T-cell receptor is responsible both for its assembly with the CD3 delta chain and for rapid degradation of the unassembled chain within the endoplasmic reticulum. The determinant for both assembly and degradation is located in a segment of eight residues containing two basic amino acids. 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/351414a0