7SR3

Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDL

7SR3 の概要

• エントリーDOI: 10.2210/pdb7sr3/pdb
• 分子名称: Protein E7 peptide,Beta-2-microglobulin,MHC class I antigen chimera, VHH (3 entities in total)
• 機能のキーワード: hla, vhh, hpv, sct, immune system
• 由来する生物種: Human papillomavirus type 16; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 121077.24

構造登録者

Finton, K.A.K.,Rupert, P.B. (登録日: 2021-11-07, 公開日: 2022-11-23, 最終更新日: 2024-10-16)

主引用文献

Finton, K.A.K.,Rupert, P.B.,Friend, D.J.,Dinca, A.,Lovelace, E.S.,Buerger, M.,Rusnac, D.V.,Foote-McNabb, U.,Chour, W.,Heath, J.R.,Campbell, J.S.,Pierce, R.H.,Strong, R.K.
Effects of HLA single chain trimer design on peptide presentation and stability.
Front Immunol, 14:1170462-1170462, 2023

PubMed Abstract: MHC class I "" molecules, coupling MHC heavy chain, β-microglobulin, and a specific peptide into a single polypeptide chain, are widely used in research. To more fully understand caveats associated with this design that may affect its use for basic and translational studies, we evaluated a set of engineered single-chain trimers with combinations of stabilizing mutations across eight different classical and non-classical human class I alleles with 44 different peptides, including a novel human/murine chimeric design. While, overall, single-chain trimers accurately recapitulate native molecules, care was needed in selecting designs for studying peptides longer or shorter than 9-mers, as single-chain trimer design could affect peptide conformation. In the process, we observed that of peptide binding were often discordant with and that yields and stabilities varied widely with construct design. We also developed novel reagents to improve the crystallizability of these proteins and confirmed novel modes of peptide presentation.

PubMed: 37207206
DOI: 10.3389/fimmu.2023.1170462

実験手法

X-RAY DIFFRACTION (2.49 Å)