4MVB

42F3 pCPB7/H-2Ld Complex

Summary for 4MVB

• Entry DOI: 10.2210/pdb4mvb/pdb
• Related: 3TF7 3TFK 3TJH 3TPU 4MS8
• Descriptor: 42F3 alpha VmCh, 42F3 beta VmCh, H-2 class I histocompatibility antigen, L-D alpha chain, ... (4 entities in total)
• Functional Keywords: ig, tcr, mhc, immune system
• Biological source: Mus musculus, Homo sapiens (mouse, human); More
• Total number of polymer chains: 4
• Total formula weight: 72693.42

Authors

Birnbaum, M.E.,Adams, J.J.,Garcia, K.C. (deposition date: 2013-09-23, release date: 2015-08-19, Last modification date: 2024-11-06)

Primary citation

Adams, J.J.,Narayanan, S.,Birnbaum, M.E.,Sidhu, S.S.,Blevins, S.J.,Gee, M.H.,Sibener, L.V.,Baker, B.M.,Kranz, D.M.,Garcia, K.C.
Structural interplay between germline interactions and adaptive recognition determines the bandwidth of TCR-peptide-MHC cross-reactivity.
Nat. Immunol., 17:87-94, 2016

PubMed Abstract: The T cell antigen receptor (TCR)-peptide-major histocompatibility complex (MHC) interface is composed of conserved and diverse regions, yet the relative contribution of each in shaping recognition by T cells remains unclear. Here we isolated cross-reactive peptides with limited homology, which allowed us to compare the structural properties of nine peptides for a single TCR-MHC pair. The TCR's cross-reactivity was rooted in highly similar recognition of an apical 'hot-spot' position in the peptide with tolerance of sequence variation at ancillary positions. Furthermore, we found a striking structural convergence onto a germline-mediated interaction between the TCR CDR1α region and the MHC α2 helix in twelve TCR-peptide-MHC complexes. Our studies suggest that TCR-MHC germline-mediated constraints, together with a focus on a small peptide hot spot, might place limits on peptide antigen cross-reactivity.

PubMed: 26523866
DOI: 10.1038/ni.3310

Experimental method

X-RAY DIFFRACTION (3.088 Å)