1YJD

Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)

Summary for 1YJD

• Entry DOI: 10.2210/pdb1yjd/pdb
• Descriptor: Fab fragment of 5.11A1 antibody light chain, Fab fragment of 5.11A1 antibody heavy chain, T-cell-specific surface glycoprotein CD28, ... (5 entities in total)
• Functional Keywords: igsf, cd28 homodimer, immune system-signaling protein complex, immune system/signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P10747
• Total number of polymer chains: 3
• Total formula weight: 63945.46

Authors

Evans, E.J.,Esnouf, R.M.,Manso-Sancho, R.,Gilbert, R.J.C.,James, J.R.,Sorensen, P.,Stuart, D.I.,Davis, S.J. (deposition date: 2005-01-14, release date: 2005-02-15, Last modification date: 2020-07-29)

Primary citation

Evans, E.J.,Esnouf, R.M.,Manso-Sancho, R.,Gilbert, R.J.C.,James, J.R.,Yu, C.,Fennelly, J.A.,Vowles, C.,Hanke, T.,Walse, B.,Hunig, T.,Sorensen, P.,Stuart, D.I.,Davis, S.J.
Crystal structure of a soluble CD28-Fab complex
Nat.Immunol., 6:271-279, 2005

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 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.

PubMed: 15696168
DOI: 10.1038/ni1170

Experimental method

X-RAY DIFFRACTION (2.7 Å)