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2AK4

Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide

2AK4 の概要
エントリーDOI10.2210/pdb2ak4/pdb
関連するPDBエントリー1ZHL
分子名称HLA-B35 variant, Beta-2-microglobulin, EBV peptide LPEPLPQGQLTAY, ... (7 entities in total)
機能のキーワードt cell receptor, bulged epitopes, pmhc-tcr complex, immune system
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Secreted: P61769
タンパク質・核酸の鎖数20
化学式量合計390028.74
構造登録者
主引用文献Tynan, F.E.,Burrows, S.R.,Buckle, A.M.,Clements, C.S.,Borg, N.A.,Miles, J.J.,Beddoe, T.,Whisstock, J.C.,Wilce, M.C.,Silins, S.L.,Burrows, J.M.,Kjer-Nielsen, L.,Kostenko, L.,Purcell, A.W.,McCluskey, J.,Rossjohn, J.
T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide
Nat.Immunol., 6:1114-1122, 2005
Cited by
PubMed Abstract: Unusually long major histocompatibility complex (MHC) class I-restricted epitopes are important in immunity, but their 'bulged' conformation represents a potential obstacle to alphabeta T cell receptor (TCR)-MHC class I docking. To elucidate how such recognition is achieved while still preserving MHC restriction, we have determined here the structure of a TCR in complex with HLA-B(*)3508 presenting a peptide 13 amino acids in length. This complex was atypical of TCR-peptide-MHC class I interactions, being dominated at the interface by peptide-mediated interactions. The TCR assumed two distinct orientations, swiveling on top of the centrally bulged, rigid peptide such that only limited contacts were made with MHC class I. Although the TCR-peptide recognition resembled an antibody-antigen interaction, the TCR-MHC class I contacts defined a minimal 'generic footprint' of MHC-restriction. Thus our findings simultaneously demonstrate the considerable adaptability of the TCR and the 'shape' of MHC restriction.
PubMed: 16186824
DOI: 10.1038/ni1257
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 2ak4
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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