3RDT

Crystal Structure of 809.B5 TCR complexed with MHC Class II I-Ab/3k peptide

Summary for 3RDT

• Entry DOI: 10.2210/pdb3rdt/pdb
• Related: 1LNU 3C5Z 3C60 3C6L
• Descriptor: H-2 class II histocompatibility antigen, A-B alpha chain, 3K peptide, linker and MHC H-2 class II I-Ab beta chain, TCR 809.B5 alpha chain, ... (4 entities in total)
• Functional Keywords: mhc, tcr, immune receptor, ig-like domain, immune system
• Biological source: Mus musculus (mouse); More
• Cellular location: Membrane ; Single-pass type I membrane protein : P14434
• Total number of polymer chains: 4
• Total formula weight: 95597.18

Authors

Trenh, P.,Huseby, E.S.,Stern, L.J. (deposition date: 2011-04-01, release date: 2011-12-07, Last modification date: 2024-10-30)

Primary citation

Stadinski, B.D.,Trenh, P.,Smith, R.L.,Bautista, B.,Huseby, P.G.,Li, G.,Stern, L.J.,Huseby, E.S.
A role for differential variable gene pairing in creating T cell receptors specific for unique major histocompatibility ligands.
Immunity, 35:694-704, 2011

PubMed Abstract: A limited set of T cell receptor (TCR) variable (V) gene segments are used to create a repertoire of TCRs that recognize all major histocompatibility complex (MHC) ligands within a species. How individual αβTCRs are constructed to specifically recognize a limited set of MHC ligands is unclear. Here we have identified a role for the differential pairing of particular V gene segments in creating TCRs that recognized MHC class II ligands exclusively, or cross-reacted with classical and nonclassical MHC class I ligands. Biophysical and structural experiments indicated that TCR specificity for MHC ligands is not driven by germline-encoded pairwise interactions.Rather, identical TCRβ chains can have altered peptide-MHC (pMHC) binding modes when paired with different TCRα chains. The ability of TCR chain pairing to modify how V region residues interact with pMHC helps to explain how the same V genes are used to create TCRs specific for unique MHC ligands.

PubMed: 22101158
DOI: 10.1016/j.immuni.2011.10.012

Experimental method

X-RAY DIFFRACTION (2.7 Å)