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PDBsum entry 4d0d

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protein ligands Protein-protein interface(s) links
Immune system PDB id
4d0d

 

 

 

 

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Contents
Protein chains
275 a.a.
96 a.a.
Ligands
VAL-ILE-PHE-PRO-
ALA-LYS-SER-LEU
×4
Waters ×9
PDB id:
4d0d
Name: Immune system
Title: Complex of a b2 chicken mhc class i molecule and a 8mer chicken peptide
Structure: Major histocompatibility complex class i glycoprotein haplotype b2. Chain: a, d, g, j. Fragment: extracellular domains, residues 22-293. Engineered: yes. Beta-2-microglobulin. Chain: b, e, h, k. Fragment: residues 22-119. Engineered: yes.
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss rosetta. Other_details: b2 haplotype. Synthetic: yes. Organism_taxid: 9031
Resolution:
3.13Å     R-factor:   0.293     R-free:   0.299
Authors: P.E.Chappell,P.Roversi,M.C.Harrison,L.E.Mears,J.F.Kaufman,S.M.Lea
Key ref: P.Chappell et al. (2015). Expression levels of MHC class I molecules are inversely correlated with promiscuity of peptide binding. Elife, 4, e05345. PubMed id: 25860507 DOI: 10.7554/eLife.05345
Date:
25-Apr-14     Release date:   06-May-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O46789  (O46789_CHICK) -  MHC class I alpha chain 2 from Gallus gallus
Seq:
Struc:
355 a.a.
275 a.a.*
Protein chains
Pfam   ArchSchema ?
P21611  (B2MG_CHICK) -  Beta-2-microglobulin from Gallus gallus
Seq:
Struc:
119 a.a.
96 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
DOI no: 10.7554/eLife.05345 Elife 4:e05345 (2015)
PubMed id: 25860507  
 
 
Expression levels of MHC class I molecules are inversely correlated with promiscuity of peptide binding.
P.Chappell, e.l. .K.Meziane, M.Harrison, ..Magiera, C.Hermann, L.Mears, A.G.Wrobel, C.Durant, L.L.Nielsen, S.Buus, N.Ternette, W.Mwangi, C.Butter, V.Nair, T.Ahyee, R.Duggleby, A.Madrigal, P.Roversi, S.M.Lea, J.Kaufman.
 
  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.
 

 

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