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Crystal structure of the Vα domain of a T cell antigen receptor

Crystal structure of the Vα domain of a T cell antigen receptor
Crystal structure of the Vα domain of a T cell antigen receptor

The crystal structure of the Vα domain of a T cell antigen receptor (TCR) was determined at a resolution of 2.2 angstroms. This structure represents an immunoglobulin topology set different from those previously described. A switch in a polypeptide strand from one β sheet to the other enables a pair of Vα homodimers to pack together to form a tetramer, such that the homodimers are parallel to each other and all hypervariable loops face in one direction. On the basis of the observed mode of Vα association, a model of an (αβ)2 TCR tetramer can be positioned relative to the major histocompatibility complex class II (αβ)2 tetramer with the third hypervariable loop of Vα over the amino-terminal portion of the antigenic peptide and the corresponding loop of Vβ over its carboxyl-terminal residues. TCR dimerization that is mediated by the α chain may contribute to the coupling of antigen recognition to signal transduction during T cell activation.

0036-8075
1821
Fields, Barry A.
737f0eac-df6f-4433-9977-6297daa487a7
Ober, Bertram
fdc0003e-6a7a-4894-bd4a-32d9d27f7c93
Malchiodi, Emilio L.
362ae1fc-a193-46b3-af63-7300ad85d2e0
Lebedeva, Marina I.
b150ad1a-0c37-4bb9-b908-79e95ba08744
Braden, Bradford C.
2e707283-49e9-4d52-ae27-2b47f85376db
Ysern, Xavier
b185288d-519f-41cf-b20f-f7f3c9d85d40
Kim, Jin Kyoo
3f679975-b86c-4b96-9571-499c2ad80378
Shao, Xuguang
02d0b239-e3a1-4d8c-a7cd-07670b56969d
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Mariuzza, Roy A.
e81103c5-af20-4034-8d29-0c24b2a98b40
Fields, Barry A.
737f0eac-df6f-4433-9977-6297daa487a7
Ober, Bertram
fdc0003e-6a7a-4894-bd4a-32d9d27f7c93
Malchiodi, Emilio L.
362ae1fc-a193-46b3-af63-7300ad85d2e0
Lebedeva, Marina I.
b150ad1a-0c37-4bb9-b908-79e95ba08744
Braden, Bradford C.
2e707283-49e9-4d52-ae27-2b47f85376db
Ysern, Xavier
b185288d-519f-41cf-b20f-f7f3c9d85d40
Kim, Jin Kyoo
3f679975-b86c-4b96-9571-499c2ad80378
Shao, Xuguang
02d0b239-e3a1-4d8c-a7cd-07670b56969d
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Mariuzza, Roy A.
e81103c5-af20-4034-8d29-0c24b2a98b40

Fields, Barry A., Ober, Bertram, Malchiodi, Emilio L., Lebedeva, Marina I., Braden, Bradford C., Ysern, Xavier, Kim, Jin Kyoo, Shao, Xuguang, Ward, E. Sally and Mariuzza, Roy A. (1995) Crystal structure of the Vα domain of a T cell antigen receptor. Science, 270 (5243), 1821. (doi:10.1126/science.270.5243.1821).

Record type: Article

Abstract

The crystal structure of the Vα domain of a T cell antigen receptor (TCR) was determined at a resolution of 2.2 angstroms. This structure represents an immunoglobulin topology set different from those previously described. A switch in a polypeptide strand from one β sheet to the other enables a pair of Vα homodimers to pack together to form a tetramer, such that the homodimers are parallel to each other and all hypervariable loops face in one direction. On the basis of the observed mode of Vα association, a model of an (αβ)2 TCR tetramer can be positioned relative to the major histocompatibility complex class II (αβ)2 tetramer with the third hypervariable loop of Vα over the amino-terminal portion of the antigenic peptide and the corresponding loop of Vβ over its carboxyl-terminal residues. TCR dimerization that is mediated by the α chain may contribute to the coupling of antigen recognition to signal transduction during T cell activation.

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Published date: 15 December 1995

Identifiers

Local EPrints ID: 425111
URI: https://eprints.soton.ac.uk/id/eprint/425111
ISSN: 0036-8075
PURE UUID: 20f2c083-2b80-41fb-b79b-e5bf46154851
ORCID for E. Sally Ward: ORCID iD orcid.org/0000-0003-3232-7238

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Date deposited: 11 Oct 2018 16:30
Last modified: 22 May 2019 00:21

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Contributors

Author: Barry A. Fields
Author: Bertram Ober
Author: Emilio L. Malchiodi
Author: Marina I. Lebedeva
Author: Bradford C. Braden
Author: Xavier Ysern
Author: Jin Kyoo Kim
Author: Xuguang Shao
Author: E. Sally Ward ORCID iD
Author: Roy A. Mariuzza

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