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PDBsum entry 3bew

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protein ligands Protein-protein interface(s) links
Immune system PDB id
3bew
Jmol
Contents
Protein chains
271 a.a. *
99 a.a. *
Ligands
ARG-GLU-VAL-ASP-
GLU-GLN-LEU-LEU-
SER-VAL
×2
Waters ×128
* Residue conservation analysis
PDB id:
3bew
Name: Immune system
Title: 10mer crystal structure of chicken mhc class i haplotype b21
Structure: Major histocompatibility complex class i glycoprotein haplotype b21. Chain: a, d. Fragment: unp residues 1-270. Synonym: mhc class i molecule precursor, mhc class i alpha chain 2, mhc class i antigen, mhc class i glycoprotein. Engineered: yes. Beta-2-microglobulin. Chain: b, e.
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Strain: b21. Gene: bfiv21, b-fiv, bf2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: b2m. Synthetic: yes.
Resolution:
2.60Å     R-factor:   0.237     R-free:   0.295
Authors: M.Koch,S.Camp,T.Collen,D.Avila,J.Salomonsen,H.J.Wallny, A.Van Hateren,L.Hunt,J.P.Jacob,F.Johnston,D.A.Marston, I.Shaw,P.R.Dunbar,V.Cerundolo,E.Y.Jones,J.Kaufman
Key ref: M.Koch et al. (2007). Structures of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding. Immunity, 27, 885-899. PubMed id: 18083574
Date:
20-Nov-07     Release date:   01-Jan-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q95601  (Q95601_CHICK) -  MHC class I alpha chain 2
Seq:
Struc:
355 a.a.
271 a.a.*
Protein chains
Pfam   ArchSchema ?
P21611  (B2MG_CHICK) -  Beta-2-microglobulin
Seq:
Struc:
119 a.a.
99 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   8 terms 
  Biological process     immune system process   10 terms 
  Biochemical function     peptide antigen binding     2 terms  

 

 
Immunity 27:885-899 (2007)
PubMed id: 18083574  
 
 
Structures of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding.
M.Koch, S.Camp, T.Collen, D.Avila, J.Salomonsen, H.J.Wallny, A.van Hateren, L.Hunt, J.P.Jacob, F.Johnston, D.A.Marston, I.Shaw, P.R.Dunbar, V.Cerundolo, E.Y.Jones, J.Kaufman.
 
  ABSTRACT  
 
Little is known about the structure of major histocompatibility complex (MHC) molecules outside of mammals. Only one class I molecule in the chicken MHC is highly expressed, leading to strong genetic associations with infectious pathogens. Here, we report two structures of the MHC class I molecule BF2*2101 from the B21 haplotype, which is known to confer resistance to Marek's disease caused by an oncogenic herpesvirus. The binding groove has an unusually large central cavity, which confers substantial conformational flexibility to the crucial residue Arg9, allowing remodeling of key peptide-binding sites. The coupled variation of anchor residues from the peptide, utilizing a charge-transfer system unprecedented in MHC molecules, allows peptides with conspicuously different sequences to be bound. This promiscuous binding extends our understanding of ways in which MHC class I molecules can present peptides to the immune system and might explain the resistance of the B21 haplotype to Marek's disease.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21327606 A.Cloutier, J.A.Mills, and A.J.Baker (2011).
Characterization and locus-specific typing of MHC class I genes in the red-billed gull (Larus scopulinus) provides evidence for major, minor, and nonclassical loci.
  Immunogenetics, 63, 377-394.  
21151886 C.S.Hee, S.Gao, B.Loll, M.M.Miller, B.Uchanska-Ziegler, O.Daumke, and A.Ziegler (2010).
Structure of a classical MHC class I molecule that binds "non-classical" ligands.
  PLoS Biol, 8, e1000557.
PDB codes: 3p73 3p77
20976198 I.K.Macdonald, M.Harkiolaki, L.Hunt, T.Connelley, A.V.Carroll, N.D.MacHugh, S.P.Graham, E.Y.Jones, W.I.Morrison, D.R.Flower, and S.A.Ellis (2010).
MHC class I bound to an immunodominant Theileria parva epitope demonstrates unconventional presentation to T cell receptors.
  PLoS Pathog, 6, e1001149.
PDB code: 2xfx
20618767 Y.C.Jin, P.Wei, X.X.Wei, Z.Y.Zhao, and Y.Li (2010).
Rapid detection of BF haplotypes by a semi-nested polymerase chain reaction, which causes resistance/susceptibility to Marek's disease in chicken.
  Scand J Immunol, 72, 94-97.  
  19342797 C.S.Hee, S.Gao, M.M.Miller, R.M.Goto, A.Ziegler, O.Daumke, and B.Uchanska-Ziegler (2009).
Expression, purification and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule YF1*7.1.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 422-425.  
19452149 M.Promerová, T.Albrecht, and J.Bryja (2009).
Extremely high MHC class I variation in a population of a long-distance migrant, the Scarlet Rosefinch (Carpodacus erythrinus).
  Immunogenetics, 61, 451-461.  
19805366 R.M.Goto, Y.Wang, R.L.Taylor, P.S.Wakenell, K.Hosomichi, T.Shiina, C.S.Blackmore, W.E.Briles, and M.M.Miller (2009).
BG1 has a major role in MHC-linked resistance to malignant lymphoma in the chicken.
  Proc Natl Acad Sci U S A, 106, 16740-16745.  
19004781 D.M.Zajonc, H.Striegl, C.C.Dascher, and I.A.Wilson (2008).
The crystal structure of avian CD1 reveals a smaller, more primordial antigen-binding pocket compared to mammalian CD1.
  Proc Natl Acad Sci U S A, 105, 17925-17930.
PDB code: 3dbx
18612635 M.A.Sherman, R.M.Goto, R.E.Moore, H.D.Hunt, T.D.Lee, and M.M.Miller (2008).
Mass spectral data for 64 eluted peptides and structural modeling define peptide binding preferences for class I alleles in two chicken MHC-B haplotypes associated with opposite responses to Marek's disease.
  Immunogenetics, 60, 527-541.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.