2CKB

STRUCTURE OF THE 2C/KB/DEV8 COMPLEX

2CKB の概要

• エントリーDOI: 10.2210/pdb2ckb/pdb
• 分子名称: ALPHA, BETA T CELL RECEPTOR, MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I MOLECULE K(B), DEV8 PEPTIDE, ... (6 entities in total)
• 機能のキーワード: t cell antigen receptor, major histocompatibility complex
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01901; Secreted: P01887
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 185999.84

構造登録者

Garcia, K.C.,Degano, M.,Wilson, I.A. (登録日: 1998-01-14, 公開日: 1998-04-29, 最終更新日: 2024-10-30)

主引用文献

Garcia, K.C.,Degano, M.,Pease, L.R.,Huang, M.,Peterson, P.A.,Teyton, L.,Wilson, I.A.
Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen.
Science, 279:1166-1172, 1998

PubMed Abstract: The T cell receptor (TCR) inherently has dual specificity. T cells must recognize self-antigens in the thymus during maturation and then discriminate between foreign pathogens in the periphery. A molecular basis for this cross-reactivity is elucidated by the crystal structure of the alloreactive 2C TCR bound to self peptide-major histocompatibility complex (pMHC) antigen H-2Kb-dEV8 refined against anisotropic 3.0 angstrom resolution x-ray data. The interface between peptide and TCR exhibits extremely poor shape complementarity, and the TCR beta chain complementarity-determining region 3 (CDR3) has minimal interaction with the dEV8 peptide. Large conformational changes in three of the TCR CDR loops are induced upon binding, providing a mechanism of structural plasticity to accommodate a variety of different peptide antigens. Extensive TCR interaction with the pMHC alpha helices suggests a generalized orientation that is mediated by the Valpha domain of the TCR and rationalizes how TCRs can effectively "scan" different peptides bound within a large, low-affinity MHC structural framework for those that provide the slight additional kinetic stabilization required for signaling.

PubMed: 9469799
DOI: 10.1126/science.279.5354.1166

実験手法

X-RAY DIFFRACTION (3 Å)