2K4F

Mouse CD3epsilon Cytoplasmic Tail

Summary for 2K4F

• Entry DOI: 10.2210/pdb2k4f/pdb
• Descriptor: T-cell surface glycoprotein CD3 epsilon chain (1 entity in total)
• Functional Keywords: itam, tcr, cd3e, membrane bound protein, bicelle, immunoglobulin domain, membrane, phosphoprotein, receptor, transmembrane, immune system, signaling protein
• Biological source: Mus musculus (mouse)
• Cellular location: Membrane; Single-pass type I membrane protein: P22646
• Total number of polymer chains: 1
• Total formula weight: 6313.18

Authors

Xu, C.,Call, M.E.,Schwieters, C.D.,Schnell, J.R.,Gagnon, E.E.,Wucherpfennig, K.W.,Chou, J.J. (deposition date: 2008-06-07, release date: 2008-12-02, Last modification date: 2024-05-29)

Primary citation

Xu, C.,Gagnon, E.,Call, M.E.,Schnell, J.R.,Schwieters, C.D.,Carman, C.V.,Chou, J.J.,Wucherpfennig, K.W.
Regulation of T Cell Receptor Activation by Dynamic Membrane Binding of the CD3varepsilon Cytoplasmic Tyrosine-Based Motif.
Cell(Cambridge,Mass.), 135:702-713, 2008

PubMed Abstract: Many immune system receptors signal through cytoplasmic tyrosine-based motifs (ITAMs), but how receptor ligation results in ITAM phosphorylation remains unknown. Live-cell imaging studies showed a close interaction of the CD3epsilon cytoplasmic domain of the T cell receptor (TCR) with the plasma membrane through fluorescence resonance energy transfer between a C-terminal fluorescent protein and a membrane fluorophore. Electrostatic interactions between basic CD3epsilon residues and acidic phospholipids enriched in the inner leaflet of the plasma membrane were required for binding. The nuclear magnetic resonance structure of the lipid-bound state of this cytoplasmic domain revealed deep insertion of the two key tyrosines into the hydrophobic core of the lipid bilayer. Receptor ligation thus needs to result in unbinding of the CD3epsilon ITAM from the membrane to render these tyrosines accessible to Src kinases. Sequestration of key tyrosines into the lipid bilayer represents a previously unrecognized mechanism for control of receptor activation.

PubMed: 19013279
DOI: 10.1016/j.cell.2008.09.044

Experimental method

SOLUTION NMR