Summary for 4D0C
| Entry DOI | 10.2210/pdb4d0c/pdb |
| Related | 4D0B 4D0D |
| Descriptor | MHC CLASS I ALPHA CHAIN 2, BETA-2-MICROGLOBULIN, 10MER PEPTIDE, ... (5 entities in total) |
| Functional Keywords | immune system |
| Biological source | GALLUS GALLUS (CHICKEN) More |
| Total number of polymer chains | 3 |
| Total formula weight | 49111.66 |
| Authors | Chappell, P.E.,Roversi, P.,Harrison, M.C.,Mears, L.E.,Kaufman, J.F.,Lea, S.M. (deposition date: 2014-04-25, release date: 2015-05-06, Last modification date: 2024-11-06) |
| Primary citation | Chappell, P.,Meziane, E.K.,Harrison, M.,Magiera, L.,Hermann, C.,Mears, L.,Wrobel, A.G.,Durant, C.,Nielsen, L.L.,Buus, S.,Ternette, N.,Mwangi, W.,Butter, C.,Nair, V.,Ahyee, T.,Duggleby, R.,Madrigal, A.,Roversi, P.,Lea, S.M.,Kaufman, J. Expression levels of MHC class I molecules are inversely correlated with promiscuity of peptide binding. Elife, 4:e05345-e05345, 2015 Cited by PubMed Abstract: Highly polymorphic major histocompatibility complex (MHC) molecules are at the heart of adaptive immune responses, playing crucial roles in many kinds of disease and in vaccination. We report that breadth of peptide presentation and level of cell surface expression of class I molecules are inversely correlated in both chickens and humans. This relationship correlates with protective responses against infectious pathogens including Marek's disease virus leading to lethal tumours in chickens and human immunodeficiency virus infection progressing to AIDS in humans. We propose that differences in peptide binding repertoire define two groups of MHC class I molecules strategically evolved as generalists and specialists for different modes of pathogen resistance. We suggest that differences in cell surface expression level ensure the development of optimal peripheral T cell responses. The inverse relationship of peptide repertoire and expression is evidently a fundamental property of MHC molecules, with ramifications extending beyond immunology and medicine to evolutionary biology and conservation. PubMed: 25860507DOI: 10.7554/eLife.05345 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.81 Å) |
Structure validation
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