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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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| Published in: | Nature (London) 1991-05, Vol.351 (6325), p.414-416 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 416 |
| container_issue | 6325 |
| container_start_page | 414 |
| container_title | Nature (London) |
| container_volume | 351 |
| creator | COSSON, P LANKFORD, S. P BONIFACINO, J. S KLAUSNER, R. D |
| description | 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. |
| doi_str_mv | 10.1038/351414a0 |
| format | article |
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P ; BONIFACINO, J. S ; KLAUSNER, R. D</creator><creatorcontrib>COSSON, P ; LANKFORD, S. P ; BONIFACINO, J. S ; KLAUSNER, R. D</creatorcontrib><description>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.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/351414a0</identifier><identifier>PMID: 1827877</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>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</subject><ispartof>Nature (London), 1991-05, Vol.351 (6325), p.414-416</ispartof><rights>1991 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. 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P</au><au>BONIFACINO, J. S</au><au>KLAUSNER, R. D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Membrane protein association by potential intramembrane charge pairs</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>1991-05-30</date><risdate>1991</risdate><volume>351</volume><issue>6325</issue><spage>414</spage><epage>416</epage><pages>414-416</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>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.</abstract><cop>London</cop><pub>Nature Publishing</pub><pmid>1827877</pmid><doi>10.1038/351414a0</doi><tpages>3</tpages></addata></record> |
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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1991-05, Vol.351 (6325), p.414-416 |
| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | Nature Journals |
| 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 |
| title | Membrane protein association by potential intramembrane charge pairs |
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