4X5W
HLA-DR1 with CLIP102-120(M107W)
Summary for 4X5W
| Entry DOI | 10.2210/pdb4x5w/pdb |
| Descriptor | HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DRB1-1 beta chain, HLA class II histocompatibility antigen gamma chain, ... (4 entities in total) |
| Functional Keywords | mhc ii, immune system, self antigen, invariant chain, clip |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P01903 P04229 Cell membrane ; Single-pass type II membrane protein : P04233 |
| Total number of polymer chains | 3 |
| Total formula weight | 47642.79 |
| Authors | Guenther, S.,Freund, C. (deposition date: 2014-12-06, release date: 2016-03-09, Last modification date: 2024-11-13) |
| Primary citation | Wieczorek, M.,Sticht, J.,Stolzenberg, S.,Gunther, S.,Wehmeyer, C.,El Habre, Z.,Alvaro-Benito, M.,Noe, F.,Freund, C. MHC class II complexes sample intermediate states along the peptide exchange pathway. Nat Commun, 7:13224-13224, 2016 Cited by PubMed Abstract: The presentation of peptide-MHCII complexes (pMHCIIs) for surveillance by T cells is a well-known immunological concept in vertebrates, yet the conformational dynamics of antigen exchange remain elusive. By combining NMR-detected H/D exchange with Markov modelling analysis of an aggregate of 275 microseconds molecular dynamics simulations, we reveal that a stable pMHCII spontaneously samples intermediate conformations relevant for peptide exchange. More specifically, we observe two major peptide exchange pathways: the kinetic stability of a pMHCII's ground state defines its propensity for intrinsic peptide exchange, while the population of a rare, intermediate conformation correlates with the propensity of the HLA-DM-catalysed pathway. Helix-destabilizing mutants designed based on our model shift the exchange behaviour towards the HLA-DM-catalysed pathway and further allow us to conceptualize how allelic variation can shape an individual's MHC restricted immune response. PubMed: 27827392DOI: 10.1038/ncomms13224 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.34 Å) |
Structure validation
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