An alternative conformation of the T-cell receptor alpha constant region.
Alphabeta T-cell receptors (TcRs) play a central role in cellular immune response. They are members of the Ig superfamily, with extracellular regions of the alpha and beta chains each comprising a V-type domain and a C-type domain. We have determined the ectodomain structure of an alphabeta TcR, whi...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2010
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| _version_ | 1797056124883566592 |
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| author | van Boxel, G Holmes, S Fugger, L Jones, E |
| author_facet | van Boxel, G Holmes, S Fugger, L Jones, E |
| author_sort | van Boxel, G |
| collection | OXFORD |
| description | Alphabeta T-cell receptors (TcRs) play a central role in cellular immune response. They are members of the Ig superfamily, with extracellular regions of the alpha and beta chains each comprising a V-type domain and a C-type domain. We have determined the ectodomain structure of an alphabeta TcR, which recognizes the autoantigen myelin basic protein. The 2.0-A-resolution structure reveals canonical main-chain conformations for the V(alpha), V(beta), and C(beta) domains, but the C(alpha) domain exhibits a main-chain conformation remarkably different from those previously reported for TcR crystal structures. The global IgC-like fold is maintained, but a piston-like rearrangement between BC and DE beta-turns results in beta-strand slippage. This substantial conformational change may represent a signaling intermediate. Our structure is the first example for the Ig fold of the increasingly recognized concept of "metamorphic proteins." |
| first_indexed | 2024-03-06T19:18:57Z |
| format | Journal article |
| id | oxford-uuid:1963c30c-ebd9-40e6-8f07-f9f703b4e4b5 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:18:57Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:1963c30c-ebd9-40e6-8f07-f9f703b4e4b52022-03-26T10:48:46ZAn alternative conformation of the T-cell receptor alpha constant region.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1963c30c-ebd9-40e6-8f07-f9f703b4e4b5EnglishSymplectic Elements at Oxford2010van Boxel, GHolmes, SFugger, LJones, EAlphabeta T-cell receptors (TcRs) play a central role in cellular immune response. They are members of the Ig superfamily, with extracellular regions of the alpha and beta chains each comprising a V-type domain and a C-type domain. We have determined the ectodomain structure of an alphabeta TcR, which recognizes the autoantigen myelin basic protein. The 2.0-A-resolution structure reveals canonical main-chain conformations for the V(alpha), V(beta), and C(beta) domains, but the C(alpha) domain exhibits a main-chain conformation remarkably different from those previously reported for TcR crystal structures. The global IgC-like fold is maintained, but a piston-like rearrangement between BC and DE beta-turns results in beta-strand slippage. This substantial conformational change may represent a signaling intermediate. Our structure is the first example for the Ig fold of the increasingly recognized concept of "metamorphic proteins." |
| spellingShingle | van Boxel, G Holmes, S Fugger, L Jones, E An alternative conformation of the T-cell receptor alpha constant region. |
| title | An alternative conformation of the T-cell receptor alpha constant region. |
| title_full | An alternative conformation of the T-cell receptor alpha constant region. |
| title_fullStr | An alternative conformation of the T-cell receptor alpha constant region. |
| title_full_unstemmed | An alternative conformation of the T-cell receptor alpha constant region. |
| title_short | An alternative conformation of the T-cell receptor alpha constant region. |
| title_sort | alternative conformation of the t cell receptor alpha constant region |
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