3MRR

Crystal Structure of MHC class I HLA-A2 molecule complexed with Human Prostaglandin Transporter decapeptide

3MRR の概要

• エントリーDOI: 10.2210/pdb3mrr/pdb
• 関連するPDBエントリー: 3GSN 3GSO 3GSQ 3GSR 3GSU 3GSV 3GSW 3GSX 3MR9 3MRB 3MRC 3MRD 3MRE 3MRF 3MRG 3MRH 3MRI 3MRJ 3MRK 3MRL 3MRM 3MRN 3MRO 3MRP 3MRQ
• 分子名称: HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, 10-meric peptide from Solute carrier organic anion transporter family member 2A1, ... (4 entities in total)
• 機能のキーワード: mhc class i, hla, immune system, immune response, decapeptide, prostaglandin transporter, tumoral peptide, melan-a analogue, mart1 analogue, self peptide
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01892; Secreted : P61769; Cell membrane; Multi-pass membrane protein: Q92959
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 46841.24

構造登録者

Reiser, J.-B.,Machillot, P.,Chouquet, A.,Debeaupuis, E.,Echasserieau, K.,Legoux, F.,Saulquin, X.,Bonneville, M.,Housset, D. (登録日: 2010-04-29, 公開日: 2011-05-25, 最終更新日: 2023-11-01)

主引用文献

Reiser, J.B.,Legoux, F.,Gras, S.,Trudel, E.,Chouquet, A.,Leger, A.,Le Gorrec, M.,Machillot, P.,Bonneville, M.,Saulquin, X.,Housset, D.
Analysis of Relationships between Peptide/MHC Structural Features and Naive T Cell Frequency in Humans.
J.Immunol., 193:5816-5826, 2014

PubMed Abstract: The structural rules governing peptide/MHC (pMHC) recognition by T cells remain unclear. To address this question, we performed a structural characterization of several HLA-A2/peptide complexes and assessed in parallel their antigenicity, by analyzing the frequency of the corresponding Ag-specific naive T cells in A2(+) and A2(-) individuals, as well as within CD4(+) and CD8(+) subsets. We were able to find a correlation between specific naive T cell frequency and peptide solvent accessibility and/or mobility for a subset of moderately prominent peptides. However, one single structural parameter of the pMHC complexes could not be identified to explain each peptide antigenicity. Enhanced pMHC antigenicity was associated with both highly biased TRAV usage, possibly reflecting favored interaction between particular pMHC complexes and germline TRAV loops, and peptide structural features allowing interactions with a broad range of permissive CDR3 loops. In this context of constrained TCR docking mode, an optimal peptide solvent exposed surface leading to an optimal complementarity with TCR interface may constitute one of the key features leading to high frequency of specific T cells. Altogether our results suggest that frequency of specific T cells depends on the fine-tuning of several parameters, the structural determinants governing TCR-pMHC interaction being just one of them.

PubMed: 25392532
DOI: 10.4049/jimmunol.1303084

実験手法

X-RAY DIFFRACTION (1.6 Å)