- PDB-1yjd: Crystal structure of human CD28 in complex with the Fab fragment ... -
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Basic information
Entry
Database: PDB / ID: 1yjd
Title
Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)
Components
Fab fragment of 5.11A1 antibody heavy chain
Fab fragment of 5.11A1 antibody light chain
T-cell-specific surface glycoprotein CD28
Keywords
IMMUNE SYSTEM/SIGNALING PROTEIN / IgSF / CD28 homodimer / IMMUNE SYSTEM-SIGNALING PROTEIN COMPLEX
Function / homology
Function and homology information
Nef mediated downregulation of CD28 cell surface expression / regulatory T cell differentiation / positive regulation of inflammatory response to antigenic stimulus / protein complex involved in cell adhesion / regulation of regulatory T cell differentiation / CD4-positive, alpha-beta T cell proliferation / positive regulation of isotype switching to IgG isotypes / negative thymic T cell selection / positive regulation of CD4-positive, alpha-beta T cell proliferation / CD28 co-stimulation ...Nef mediated downregulation of CD28 cell surface expression / regulatory T cell differentiation / positive regulation of inflammatory response to antigenic stimulus / protein complex involved in cell adhesion / regulation of regulatory T cell differentiation / CD4-positive, alpha-beta T cell proliferation / positive regulation of isotype switching to IgG isotypes / negative thymic T cell selection / positive regulation of CD4-positive, alpha-beta T cell proliferation / CD28 co-stimulation / CD28 dependent Vav1 pathway / positive regulation of interleukin-4 production / CD28 dependent PI3K/Akt signaling / positive regulation of interleukin-10 production / humoral immune response / immunological synapse / positive regulation of viral genome replication / coreceptor activity / positive regulation of T cell proliferation / T cell costimulation / T cell activation / positive regulation of interleukin-2 production / positive regulation of mitotic nuclear division / phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of cytokine production / positive regulation of translation / apoptotic signaling pathway / Constitutive Signaling by Aberrant PI3K in Cancer / PIP3 activates AKT signaling / T cell receptor signaling pathway / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / protease binding / transcription by RNA polymerase II / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell surface receptor signaling pathway / external side of plasma membrane / negative regulation of gene expression / positive regulation of gene expression / negative regulation of apoptotic process / protein kinase binding / cell surface / positive regulation of transcription by RNA polymerase II / identical protein binding / plasma membrane / cytosol Similarity search - Function
Journal: Nat Immunol / Year: 2005 Title: Crystal structure of a soluble CD28-Fab complex. 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 ...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 / 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.
History
Deposition
Jan 14, 2005
Deposition site: RCSB / Processing site: PDBJ
Revision 1.0
Feb 15, 2005
Provider: repository / Type: Initial release
Revision 1.1
Apr 30, 2008
Group: Version format compliance
Revision 1.2
Jul 13, 2011
Group: Non-polymer description / Version format compliance
L: Fab fragment of 5.11A1 antibody light chain H: Fab fragment of 5.11A1 antibody heavy chain C: T-cell-specific surface glycoprotein CD28 hetero molecules
L: Fab fragment of 5.11A1 antibody light chain H: Fab fragment of 5.11A1 antibody heavy chain C: T-cell-specific surface glycoprotein CD28 hetero molecules
L: Fab fragment of 5.11A1 antibody light chain H: Fab fragment of 5.11A1 antibody heavy chain C: T-cell-specific surface glycoprotein CD28 hetero molecules
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