Structural studies on the leukocyte co-stimulatory molecule, B7-1
B7-1 and B7-2 are glycoproteins expressed on antigen presenting cells. The binding of these molecules to the T-cell homodimers, CD28 and CTLA-4, generate 'costimulatory' and inhibitory signals in T cells, respectively. The crystal structure of the extracellular region of B7-1 (sB7-1), solv...
| Egile Nagusiak: | , , , |
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| Formatua: | Conference item |
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2001
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| _version_ | 1826296488583495680 |
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| author | Ikemizu, S Jones, E Stuart, D Davis, S |
| author_facet | Ikemizu, S Jones, E Stuart, D Davis, S |
| author_sort | Ikemizu, S |
| collection | OXFORD |
| description | B7-1 and B7-2 are glycoproteins expressed on antigen presenting cells. The binding of these molecules to the T-cell homodimers, CD28 and CTLA-4, generate 'costimulatory' and inhibitory signals in T cells, respectively. The crystal structure of the extracellular region of B7-1 (sB7-1), solved to 3 Angstrom resolution, consists of a novel combination of two Ig-like domains, one characteristic of adhesion molecules and the other previously seen only in antigen receptors. In the crystal lattice, sB7-1 unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. The structural data suggest a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4 homodimers, along with the relatively high affinity of these interactions, favours the formation of very stable inhibitory signaling complexes. |
| first_indexed | 2024-03-07T04:17:07Z |
| format | Conference item |
| id | oxford-uuid:c9c2eebc-338e-4576-85c9-809f0e618c46 |
| institution | University of Oxford |
| last_indexed | 2024-03-07T04:17:07Z |
| publishDate | 2001 |
| record_format | dspace |
| spelling | oxford-uuid:c9c2eebc-338e-4576-85c9-809f0e618c462022-03-27T07:01:53ZStructural studies on the leukocyte co-stimulatory molecule, B7-1Conference itemhttp://purl.org/coar/resource_type/c_5794uuid:c9c2eebc-338e-4576-85c9-809f0e618c46Symplectic Elements at Oxford2001Ikemizu, SJones, EStuart, DDavis, SB7-1 and B7-2 are glycoproteins expressed on antigen presenting cells. The binding of these molecules to the T-cell homodimers, CD28 and CTLA-4, generate 'costimulatory' and inhibitory signals in T cells, respectively. The crystal structure of the extracellular region of B7-1 (sB7-1), solved to 3 Angstrom resolution, consists of a novel combination of two Ig-like domains, one characteristic of adhesion molecules and the other previously seen only in antigen receptors. In the crystal lattice, sB7-1 unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. The structural data suggest a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4 homodimers, along with the relatively high affinity of these interactions, favours the formation of very stable inhibitory signaling complexes. |
| spellingShingle | Ikemizu, S Jones, E Stuart, D Davis, S Structural studies on the leukocyte co-stimulatory molecule, B7-1 |
| title | Structural studies on the leukocyte co-stimulatory molecule, B7-1 |
| title_full | Structural studies on the leukocyte co-stimulatory molecule, B7-1 |
| title_fullStr | Structural studies on the leukocyte co-stimulatory molecule, B7-1 |
| title_full_unstemmed | Structural studies on the leukocyte co-stimulatory molecule, B7-1 |
| title_short | Structural studies on the leukocyte co-stimulatory molecule, B7-1 |
| title_sort | structural studies on the leukocyte co stimulatory molecule b7 1 |
| work_keys_str_mv | AT ikemizus structuralstudiesontheleukocytecostimulatorymoleculeb71 AT jonese structuralstudiesontheleukocytecostimulatorymoleculeb71 AT stuartd structuralstudiesontheleukocytecostimulatorymoleculeb71 AT daviss structuralstudiesontheleukocytecostimulatorymoleculeb71 |