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PDBsum entry 1lo5

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protein Protein-protein interface(s) links
Immune system/toxin PDB id
1lo5
Jmol
Contents
Protein chains
179 a.a. *
188 a.a. *
13 a.a. *
233 a.a. *
Waters ×23
* Residue conservation analysis
PDB id:
1lo5
Name: Immune system/toxin
Title: Crystal structure of the d227a variant of staphylococcal enterotoxin a in complex with human mhc class ii
Structure: Hla class ii histocompatibility antigen, dr alpha chain. Chain: a. Fragment: extracellular domain. Synonym: mhc class ii (hla-dr1, dra 0101)-chain a. Engineered: yes. Hla class ii histocompatibility antigen, dr-1 beta chain. Chain: b.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this sequence is peptide from influenza virus, hemagglutinin peptide. Staphylococcus aureus.
Biol. unit: Tetramer (from PQS)
Resolution:
3.20Å     R-factor:   0.245     R-free:   0.339
Authors: K.Petersson,M.Thunnissen,G.Forsberg,B.Walse
Key ref:
K.Petersson et al. (2002). Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules. Structure, 10, 1619-1626. PubMed id: 12467569 DOI: 10.1016/S0969-2126(02)00895-X
Date:
06-May-02     Release date:   18-Dec-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01903  (DRA_HUMAN) -  HLA class II histocompatibility antigen, DR alpha chain
Seq:
Struc:
254 a.a.
179 a.a.
Protein chain
Pfam   ArchSchema ?
P04229  (2B11_HUMAN) -  HLA class II histocompatibility antigen, DRB1-1 beta chain
Seq:
Struc:
266 a.a.
188 a.a.
Protein chain
No UniProt id for this chain
Struc: 13 a.a.
Protein chain
Pfam   ArchSchema ?
P0A0L2  (ETXA_STAAU) -  Enterotoxin type A
Seq:
Struc:
257 a.a.
233 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   3 terms 
  Biological process     immune response   3 terms 
  Biochemical function     metal ion binding     2 terms  

 

 
DOI no: 10.1016/S0969-2126(02)00895-X Structure 10:1619-1626 (2002)
PubMed id: 12467569  
 
 
Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules.
K.Petersson, M.Thunnissen, G.Forsberg, B.Walse.
 
  ABSTRACT  
 
Although the biological properties of staphylococcal enterotoxin A (SEA) have been well characterized, structural insights into the interaction between SEA and major histocompatibilty complex (MHC) class II have only been obtained by modeling. Here, the crystal structure of the D227A variant of SEA in complex with human MHC class II has been determined by X-ray crystallography. SEA(D227A) exclusively binds with its N-terminal domain to the alpha chain of HLA-DR1. The ability of one SEA molecule to crosslink two MHC molecules was modeled. It shows that this SEA molecule cannot interact with the T cell receptor (TCR) while a second SEA molecule interacts with MHC. Because of its relatively low toxicity, the D227A variant of SEA is used in tumor therapy.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Ribbon Representations of the Interfaces between (A) HLA-DR1, in Green, and SEA[D227A], in Yellow, and (B) HLA-DR1, in Green, and SEB, in Cyan, as Well as Electrostatic Interaction and Hydrogen Bond Pattern of Selected Residues in the Interface

 
  The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 1619-1626) copyright 2002.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19133806 D.L.Hu, K.Omoe, H.Sashinami, K.Shinagawa, and A.Nakane (2009).
Immunization with a Nontoxic Mutant of Staphylococcal Enterotoxin A, SEAD227A, Protects against Enterotoxin-Induced Emesis in House Musk Shrews.
  J Infect Dis, 199, 302-310.  
18506495 J.Hui, Y.Cao, F.Xiao, J.Zhang, H.Li, and F.Hu (2008).
Staphylococcus aureus enterotoxin C2 mutants: biological activity assay in vitro.
  J Ind Microbiol Biotechnol, 35, 975-980.  
18282095 M.D.Dyer, T.M.Murali, and B.W.Sobral (2008).
The landscape of human proteins interacting with viruses and other pathogens.
  PLoS Pathog, 4, e32.  
17560120 E.J.Sundberg, L.Deng, and R.A.Mariuzza (2007).
TCR recognition of peptide/MHC class II complexes and superantigens.
  Semin Immunol, 19, 262-271.  
17166841 H.Li, Y.Zhao, Y.Guo, Z.Li, L.Eisele, and W.Mourad (2007).
Zinc induces dimerization of the class II major histocompatibility complex molecule that leads to cooperative binding to a superantigen.
  J Biol Chem, 282, 5991-6000.
PDB code: 2oje
17560605 S.Günther, A.K.Varma, B.Moza, K.J.Kasper, A.W.Wyatt, P.Zhu, A.K.Rahman, Y.Li, R.A.Mariuzza, J.K.McCormick, and E.J.Sundberg (2007).
A novel loop domain in superantigens extends their T cell receptor recognition site.
  J Mol Biol, 371, 210-221.
PDB codes: 2nts 2ntt
16113251 D.D.Pless, G.Ruthel, E.K.Reinke, R.G.Ulrich, and S.Bavari (2005).
Persistence of zinc-binding bacterial superantigens at the surface of antigen-presenting cells contributes to the extreme potency of these superantigens as T-cell activators.
  Infect Immun, 73, 5358-5366.  
15049778 K.Petersson, G.Forsberg, and B.Walse (2004).
Interplay between superantigens and immunoreceptors.
  Scand J Immunol, 59, 345-355.  
14962388 Y.Zhao, Z.Li, S.J.Drozd, Y.Guo, W.Mourad, and H.Li (2004).
Crystal structure of Mycoplasma arthritidis mitogen complexed with HLA-DR1 reveals a novel superantigen fold and a dimerized superantigen-MHC complex.
  Structure, 12, 277-288.
PDB code: 1r5i
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 code is shown on the right.