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1JBJ

CD3 Epsilon and gamma Ectodomain Fragment Complex in Single-Chain Construct

Summary for 1JBJ
Entry DOI10.2210/pdb1jbj/pdb
NMR InformationBMRB: 5072
DescriptorCD3 Epsilon and gamma Ectodomain Fragment Complex (1 entity in total)
Functional Keywordsbeta-sheet, c2-set immunoglobulin superfamily, h-bonded g strand pair, single-chain, immune system
Biological sourceMus musculus (house mouse)
Cellular locationMembrane; Single-pass type I membrane protein: P11942
Total number of polymer chains1
Total formula weight20632.84
Authors
Sun, Z.-Y.J.,Kim, K.S.,Wagner, G.,Reinherz, E.L. (deposition date: 2001-06-05, release date: 2001-12-05, Last modification date: 2022-02-23)
Primary citationSun, Z.J.,Kim, K.S.,Wagner, G.,Reinherz, E.L.
Mechanisms contributing to T cell receptor signaling and assembly revealed by the solution structure of an ectodomain fragment of the CD3 epsilon gamma heterodimer.
Cell(Cambridge,Mass.), 105:913-923, 2001
Cited by
PubMed Abstract: The T cell receptor (TCR) consists of genetically diverse disulfide-linked alpha and beta chains in noncovalent association with the invariant CD3 subunits. CD3 epsilon and CD3 gamma are integral components of both the TCR and pre-TCR. Here, we present the solution structure of a heterodimeric CD3 epsilon gamma ectodomain complex. A unique side-to-side hydrophobic interface between the two C2-set immunoglobulin-like domains and parallel pairing of their respective C-terminal beta strands are revealed. Mutational analysis confirms the importance of the distinctive linkage as well as the membrane proximal stalk motif (RxCxxCxE) for domain-domain association. These biochemical and structural analyses offer insights into the modular pairwise association of CD3 invariant chains. More importantly, the findings suggest how the rigidified CD3 elements participate in TCR-based signal transduction.
PubMed: 11439187
DOI: 10.1016/S0092-8674(01)00395-6
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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