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

Structural highlights

3rdt is a 4 chain structure with sequence from Mus musculus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HA2B_MOUSE

Publication Abstract from PubMed

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 alphabetaTCRs 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 TCRbeta chains can have altered peptide-MHC (pMHC) binding modes when paired with different TCRalpha 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.

A Role for Differential Variable Gene Pairing in Creating T Cell Receptors Specific for Unique Major Histocompatibility Ligands.,Stadinski BD, Trenh P, Smith RL, Bautista B, Huseby PG, Li G, Stern LJ, Huseby ES Immunity. 2011 Nov 16. PMID:22101158[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Stadinski BD, Trenh P, Smith RL, Bautista B, Huseby PG, Li G, Stern LJ, Huseby ES. A Role for Differential Variable Gene Pairing in Creating T Cell Receptors Specific for Unique Major Histocompatibility Ligands. Immunity. 2011 Nov 16. PMID:22101158 doi:10.1016/j.immuni.2011.10.012

3rdt, resolution 2.70Å

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