8HSO

CRYSTAL STRUCTURE OF A MUTANT MYLU-B-67 FOR 2.2 ANGSTROM, 52M 53Q 54Q 55P 56W DELETED

Summary for 8HSO

• Entry DOI: 10.2210/pdb8hso/pdb
• Descriptor: Ig-like domain-containing protein, Beta-2-microglobulin, PHE-PRO-GLN-SER-ALA-PRO-HIS-GLY-VAL, ... (4 entities in total)
• Functional Keywords: mhc, immunoligy, immune system transferase complex., immune system
• Biological source: Myotis lucifugus (little brown bat); More
• Total number of polymer chains: 3
• Total formula weight: 43856.66

Authors

Wang, S.Q.,Zhang, N.Z. (deposition date: 2022-12-20, release date: 2023-12-20, Last modification date: 2025-01-01)

Primary citation

Wang, S.,Zheng, L.,Wei, X.,Qu, Z.,Du, L.,Wang, S.,Zhang, N.
Amino acid insertion in Bat MHC-I enhances complex stability and augments peptide presentation.
Commun Biol, 7:586-586, 2024

PubMed Abstract: Bats serve as reservoirs for numerous zoonotic viruses, yet they typically remain asymptomatic owing to their unique immune system. Of particular significance is the MHC-I in bats, which plays crucial role in anti-viral response and exhibits polymorphic amino acid (AA) insertions. This study demonstrated that both 5AA and 3AA insertions enhance the thermal stability of the bat MHC-I complex and enrich the diversity of bound peptides in terms of quantity and length distribution, by stabilizing the 3 helix, a region prone to conformational changes during peptide loading. However, the mismatched insertion could diminish the stability of bat pMHC-I. We proposed that a suitable insertion may help bat MHC-I adapt to high body temperatures during flight while enhancing antiviral responses. Moreover, this site-specific insertions may represent a strategy of evolutionary adaptation of MHC-I molecules to fluctuations in body temperature, as similar insertions have been found in other lower vertebrates.

PubMed: 38755285
DOI: 10.1038/s42003-024-06292-5

Experimental method

X-RAY DIFFRACTION (2.1 Å)