3MFF
1F1E8hu TCR
Summary for 3MFF
| Entry DOI | 10.2210/pdb3mff/pdb |
| Descriptor | T cell receptor alpha chain, T cell receptor beta chain, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | t-cell receptor, protein metamorphism, alpha constant domain, immune system |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 100546.63 |
| Authors | van Boxel, G.I.,Holmes, S.,Fugger, L.,Jones, E.Y. (deposition date: 2010-04-02, release date: 2010-06-02, Last modification date: 2024-10-30) |
| Primary citation | van Boxel, G.I.,Holmes, S.,Fugger, L.,Jones, E.Y. An alternative conformation of the T-cell receptor alpha constant region J.Mol.Biol., 400:828-837, 2010 Cited by PubMed Abstract: Alphabeta T-cell receptors (TcRs) play a central role in cellular immune response. They are members of the Ig superfamily, with extracellular regions of the alpha and beta chains each comprising a V-type domain and a C-type domain. We have determined the ectodomain structure of an alphabeta TcR, which recognizes the autoantigen myelin basic protein. The 2.0-A-resolution structure reveals canonical main-chain conformations for the V(alpha), V(beta), and C(beta) domains, but the C(alpha) domain exhibits a main-chain conformation remarkably different from those previously reported for TcR crystal structures. The global IgC-like fold is maintained, but a piston-like rearrangement between BC and DE beta-turns results in beta-strand slippage. This substantial conformational change may represent a signaling intermediate. Our structure is the first example for the Ig fold of the increasingly recognized concept of "metamorphic proteins." PubMed: 20630474DOI: 10.1016/j.jmb.2010.05.053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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