1JBJ
CD3 Epsilon and gamma Ectodomain Fragment Complex in Single-Chain Construct
Summary for 1JBJ
Entry DOI | 10.2210/pdb1jbj/pdb |
NMR Information | BMRB: 5072 |
Descriptor | CD3 Epsilon and gamma Ectodomain Fragment Complex (1 entity in total) |
Functional Keywords | beta-sheet, c2-set immunoglobulin superfamily, h-bonded g strand pair, single-chain, immune system |
Biological source | Mus musculus (house mouse) |
Cellular location | Membrane; Single-pass type I membrane protein: P11942 |
Total number of polymer chains | 1 |
Total formula weight | 20632.84 |
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 citation | Sun, 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: 11439187DOI: 10.1016/S0092-8674(01)00395-6 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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