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4D0B

COMPLEX OF A B21 CHICKEN MHC CLASS I MOLECULE AND A 10MER CHICKEN PEPTIDE

Replaces:  2YF6
Summary for 4D0B
Entry DOI10.2210/pdb4d0b/pdb
Related4D0C 4D0D
DescriptorMHC CLASS I ANTIGEN, BETA-2-MICROGLOBULIN, PEPTIDE, ... (4 entities in total)
Functional Keywordsimmune system
Biological sourceGALLUS GALLUS (CHICKEN)
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Total number of polymer chains3
Total formula weight49092.61
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: 2024-11-13)
Primary citationChappell, 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: 25860507
DOI: 10.7554/eLife.05345
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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