3TF7

42F3 QL9/H2-Ld complex

Summary for 3TF7

• Entry DOI: 10.2210/pdb3tf7/pdb
• Related: 2oi9 3TFK 3TJH
• Descriptor: H2-Ld SBM2, QL9 peptide (QLSPFPFDL), 42F3 Mut7 scFv (42F3 alpha chain, linker, 42F3 beta chain), ... (4 entities in total)
• Functional Keywords: ig and mhc, antigen recognition, tcr-pmhc, membrane receptors, immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 8
• Total formula weight: 154432.12

Authors

Adams, J.J.,Kranz, D.M.,Garcia, K.C. (deposition date: 2011-08-15, release date: 2011-12-07, Last modification date: 2024-10-30)

Primary citation

Adams, J.J.,Narayanan, S.,Liu, B.,Birnbaum, M.E.,Kruse, A.C.,Bowerman, N.A.,Chen, W.,Levin, A.M.,Connolly, J.M.,Zhu, C.,Kranz, D.M.,Garcia, K.C.
T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex.
Immunity, 35:681-693, 2011

PubMed Abstract: T cell receptor (TCR) engagement of peptide-major histocompatibility complex (pMHC) is essential to adaptive immunity, but it is unknown whether TCR signaling responses are influenced by the binding topology of the TCR-peptide-MHC complex. We developed yeast-displayed pMHC libraries that enabled us to identify new peptide sequences reactive with a single TCR. Structural analysis showed that four peptides bound to the TCR with distinct 3D and 2D affinities using entirely different binding chemistries. Three of the peptides that shared a common docking mode, where key TCR-MHC germline interactions are preserved, induced TCR signaling. The fourth peptide failed to induce signaling and was recognized in a substantially different TCR-MHC binding mode that apparently exceeded geometric tolerances compatible with signaling. We suggest that the stereotypical TCR-MHC docking paradigm evolved from productive signaling geometries and that TCR signaling can be modulated by peptides that are recognized in alternative TCR-pMHC binding orientations.

PubMed: 22101157
DOI: 10.1016/j.immuni.2011.09.013

Experimental method

X-RAY DIFFRACTION (2.75 Å)