9QG8
Crystal structure of the great reed warbler MHC class I in complex with an 8-mer peptide
Summary for 9QG8
| Entry DOI | 10.2210/pdb9qg8/pdb |
| Descriptor | MHC class I antigen, Beta-2-microglobulin, LYS-THR-MET-MET-ALA-HIS-ASP-LEU, ... (5 entities in total) |
| Functional Keywords | mhc class i, great reed warbler, antigen presentation, immune system |
| Biological source | Acrocephalus arundinaceus (great reed warbler) More |
| Total number of polymer chains | 3 |
| Total formula weight | 47336.79 |
| Authors | Venskutonyte, R.,Lindkvist-Petersson, K. (deposition date: 2025-03-13, release date: 2025-07-23, Last modification date: 2025-11-12) |
| Primary citation | Venskutonyte, R.,Kjellstrom, S.,O'Connor, E.A.,Westerdahl, H.,Lindkvist-Petersson, K. MHC I of the Great Reed Warbler Promotes a Flat Peptide Binding Mode. Immunology, 176:508-519, 2025 Cited by PubMed Abstract: The major histocompatibility complex (MHC) plays a key role in pathogen recognition as part of the adaptive immune system. MHC I gene copy numbers in birds of the order Passeriformes (songbirds) are substantially larger compared to other birds. MHC I diversity and antigen presentation have been carefully characterised in chicken Gallus gallus of the order Galliformes; chickens express few MHC I genes and often present antigens that bulge out of the peptide binding cleft. This observation raises the question of whether MHC I presents antigens in a similar way in species with many MHC genes? Here, we present the X-ray structure of MHC I from the great reed warbler Acrocephalus arundinaceus (Acar3) a long-distance migratory songbird. Structural analysis shows that MHC I binds the antigen in a flat conformation due to a sequentially well-conserved restriction point, acting like a pair of tweezers, within the peptide binding grove, created by Arg97 and Arg155. This more stringent antigen presentation by Acar MHC I molecules may partly explain the high MHC gene copy numbers seen in the great reed warbler. PubMed: 40643222DOI: 10.1111/imm.70015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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