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PDBsum entry 4d0c

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Immune system PDB id
4d0c

 

 

 

 

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Contents
Protein chains
276 a.a.
97 a.a.
Ligands
THR-ALA-GLY-GLN-
SER-ASN-TYR-ASP-
ARG-LEU
EDO
Waters ×31
PDB id:
4d0c
Name: Immune system
Title: Complex of a b21 chicken mhc class i molecule and a 10mer chicken peptide
Structure: Mhc class i alpha chain 2. Chain: a. Fragment: extracellular domains, residues 1-291. Synonym: major histocompatibility complex class i glycoprotein haplotype b21. Engineered: yes. Beta-2-microglobulin. Chain: b. Fragment: residues 22-119.
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss rosetta cells. Other_details: b21 haplotype. Synthetic: yes. Other_details: synthetic peptide
Resolution:
2.81Å     R-factor:   0.275     R-free:   0.282
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    
Supersedes: 2yf5
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q95601  (Q95601_CHICK) -  MHC class I alpha chain 2 from Gallus gallus
Seq:
Struc:
355 a.a.
276 a.a.*
Protein chain
Pfam   ArchSchema ?
P21611  (B2MG_CHICK) -  Beta-2-microglobulin from Gallus gallus
Seq:
Struc:
119 a.a.
97 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 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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