4N0C
42F3 TCR pCPE3/H-2Ld complex
4N0C の概要
エントリーDOI | 10.2210/pdb4n0c/pdb |
関連するPDBエントリー | 3TF7 3TFK 3TJH 3TPU 4MS8 4MVB 4MXQ 4N5E |
分子名称 | H-2 class I histocompatibility antigen, L-D alpha chain, pCPE3, 42F3 VmCh alpha, ... (4 entities in total) |
機能のキーワード | ig, tcr, mhc, antigen, immune system |
由来する生物種 | Mus musculus (mouse) 詳細 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 145581.26 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 26523866DOI: 10.1038/ni.3310 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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