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-Structure paper
Title | Crystal structure of a soluble CD28-Fab complex. |
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Journal, issue, pages | Nat Immunol, Vol. 6, Issue 3, Page 271-279, Year 2005 |
Publish date | Feb 6, 2005 |
Authors | Edward J Evans / Robert M Esnouf / Raquel Manso-Sancho / Robert J C Gilbert / John R James / Chao Yu / Janet A Fennelly / Cheryl Vowles / Thomas Hanke / Björn Walse / Thomas Hünig / Poul Sørensen / David I Stuart / Simon J Davis / |
PubMed Abstract | 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 ...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. |
External links | Nat Immunol / PubMed:15696168 |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.7 - 28.0 Å |
Structure data | EMDB-1219: PDB-1yjd: |
Chemicals | ChemComp-NAG: ChemComp-HOH: |
Source |
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Keywords | IMMUNE SYSTEM/SIGNALING PROTEIN / IgSF / CD28 homodimer / IMMUNE SYSTEM-SIGNALING PROTEIN COMPLEX |