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8KB1

Crystal structure of 11JD

Summary for 8KB1
Entry DOI10.2210/pdb8kb1/pdb
DescriptorMHC class I antigen, Beta2-microglobulin, peptide of AIV, ... (4 entities in total)
Functional Keywordsmajor histocompatibility complex, anpl-uaa, immune system
Biological sourceAnas platyrhynchos (Mallard, Anas boschas)
More
Total number of polymer chains3
Total formula weight44463.42
Authors
Tang, Z.,Zhang, N. (deposition date: 2023-08-03, release date: 2024-05-29, Last modification date: 2024-11-13)
Primary citationTang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.46 Å)
Structure validation

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