Crystal structure of a soluble CD28-Fab complex.
Naive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2005
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| _version_ | 1797071138022490112 |
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| author | Evans, E Esnouf, R Manso-Sancho, R Gilbert, R James, JR Yu, C Fennelly, J Vowles, C Hanke, T Walse, B Hünig, T Sørensen, P Stuart, D Davis, S |
| author_facet | Evans, E Esnouf, R Manso-Sancho, R Gilbert, R James, JR Yu, C Fennelly, J Vowles, C Hanke, T Walse, B Hünig, T Sørensen, P Stuart, D Davis, S |
| author_sort | Evans, E |
| collection | OXFORD |
| description | Naive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. Structural comparisons redefine the evolutionary relationships of CD28-related proteins, antigen receptors and adhesion molecules and account for the distinct ligand-binding and stoichiometric properties of CD28 and the related, inhibitory homodimer CTLA-4. Cryo-electron microscopy-based comparisons of complexes of CD28 with mitogenic and nonmitogenic antibodies place new constraints on models of antibody-induced receptor triggering. This work completes the initial structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system. |
| first_indexed | 2024-03-06T22:48:56Z |
| format | Journal article |
| id | oxford-uuid:5e25d640-30dd-4d52-bb72-c5d980fcc208 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:48:56Z |
| publishDate | 2005 |
| record_format | dspace |
| spelling | oxford-uuid:5e25d640-30dd-4d52-bb72-c5d980fcc2082022-03-26T17:38:48ZCrystal structure of a soluble CD28-Fab complex.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5e25d640-30dd-4d52-bb72-c5d980fcc208EnglishSymplectic Elements at Oxford2005Evans, EEsnouf, RManso-Sancho, RGilbert, RJames, JRYu, CFennelly, JVowles, CHanke, TWalse, BHünig, TSørensen, PStuart, DDavis, SNaive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. Structural comparisons redefine the evolutionary relationships of CD28-related proteins, antigen receptors and adhesion molecules and account for the distinct ligand-binding and stoichiometric properties of CD28 and the related, inhibitory homodimer CTLA-4. Cryo-electron microscopy-based comparisons of complexes of CD28 with mitogenic and nonmitogenic antibodies place new constraints on models of antibody-induced receptor triggering. This work completes the initial structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system. |
| spellingShingle | Evans, E Esnouf, R Manso-Sancho, R Gilbert, R James, JR Yu, C Fennelly, J Vowles, C Hanke, T Walse, B Hünig, T Sørensen, P Stuart, D Davis, S Crystal structure of a soluble CD28-Fab complex. |
| title | Crystal structure of a soluble CD28-Fab complex. |
| title_full | Crystal structure of a soluble CD28-Fab complex. |
| title_fullStr | Crystal structure of a soluble CD28-Fab complex. |
| title_full_unstemmed | Crystal structure of a soluble CD28-Fab complex. |
| title_short | Crystal structure of a soluble CD28-Fab complex. |
| title_sort | crystal structure of a soluble cd28 fab complex |
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