8KB1

Crystal structure of 11JD

8KB1 の概要

• エントリーDOI: 10.2210/pdb8kb1/pdb
• 分子名称: MHC class I antigen, Beta2-microglobulin, peptide of AIV, ... (4 entities in total)
• 機能のキーワード: major histocompatibility complex, anpl-uaa, immune system
• 由来する生物種: Anas platyrhynchos (Mallard, Anas boschas); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44463.42

構造登録者

Tang, Z.,Zhang, N. (登録日: 2023-08-03, 公開日: 2024-05-29)

主引用文献

Tang, Z.,Wang, S.,Du, L.,Hu, D.,Chen, X.,Zheng, H.,Ding, H.,Chen, S.,Zhang, L.,Zhang, N.
The impact of micropolymorphism in Anpl-UAA on structural stability and peptide presentation.
Int.J.Biol.Macromol., 267:131665-131665, 2024

PubMed Abstract: Micropolymorphism significantly shapes the peptide-binding characteristics of major histocompatibility complex class I (MHC-I) molecules, affecting the host's resistance to pathogens, which is particularly pronounced in avian species displaying the "minimal essential MHC" expression pattern. In this study, we compared two duck MHC-I alleles, Anpl-UAA*77 and Anpl-UAA*78, that exhibit markedly different peptide binding properties despite their high sequence homology. Through mutagenesis experiments and crystallographic analysis of complexes with the influenza virus-derived peptide AEAIIVAMV (AEV9), we identified a critical role for the residue at position 62 in regulating hydrogen-bonding interactions between the peptide backbone and the peptide-binding groove. This modulation affects the characteristics of the B pocket and the stability of the loop region between the 3 helix and the α1 helix, leading to significant changes in the structure and stability of the peptide-MHC-I complex (pMHC-I). Moreover, the proportion of different residues at position 62 among Anpl-UAAs may reflect the correlation between pAnpl-UAA stability and duck body temperature. This research not only advances our understanding of the Anpl-UAA structure but also deepens our insight into the impact of MHC-I micropolymorphism on peptide binding.

PubMed: 38636758
DOI: 10.1016/j.ijbiomac.2024.131665

実験手法

X-RAY DIFFRACTION (2.46 Å)