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PDBsum entry 1ffp

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Immune system/signaling protein PDB id
1ffp

 

 

 

 

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Contents
Protein chains
273 a.a. *
100 a.a. *
Ligands
SER-ALA-VAL-TYR-
ASN-PHE-ALA-THR-
MET
×2
Waters ×14
* Residue conservation analysis
PDB id:
1ffp
Name: Immune system/signaling protein
Title: Crystal structure of murine class i h-2db complexed with peptide gp33 (c9m/k1s)
Structure: H-2 class i histocompatibility antigen, d-b, alpha chain. Chain: a, d. Fragment: extracellular portion. Synonym: h-2d(b). Engineered: yes. Beta-2 microglobulin beta chain. Chain: b, e. Fragment: beta-2 microglobulin. Engineered: yes.
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Synthetic: yes. Other_details: the peptide was synthesized
Biol. unit: Trimer (from PQS)
Resolution:
2.60Å     R-factor:   0.250     R-free:   0.303
Authors: B.Wang,A.Sharma,R.Maile,M.Saad,E.J.Collins,J.A.Frelinger
Key ref: B.Wang et al. (2002). Peptidic termini play a significant role in TCR recognition. J Immunol, 169, 3137-3145. PubMed id: 12218131
Date:
25-Jul-00     Release date:   11-Dec-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01899  (HA11_MOUSE) -  H-2 class I histocompatibility antigen, D-B alpha chain from Mus musculus
Seq:
Struc:
362 a.a.
273 a.a.
Protein chains
Pfam   ArchSchema ?
P01887  (B2MG_MOUSE) -  Beta-2-microglobulin from Mus musculus
Seq:
Struc:
119 a.a.
100 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
J Immunol 169:3137-3145 (2002)
PubMed id: 12218131  
 
 
Peptidic termini play a significant role in TCR recognition.
B.Wang, A.Sharma, R.Maile, M.Saad, E.J.Collins, J.A.Frelinger.
 
  ABSTRACT  
 
TCR recognition of class I MHC is dependent on the composition of the antigenic peptide and the MHC. Single amino acid substitutions in either the MHC or the peptide may dramatically alter recognition. While the major interactions between TCR and the peptide/MHC complex appear to be focused on the complementarity-determining region (CDR)3, it is also clear from the cocrystal structure of class I MHC and TCR that the amino and carboxyl ends of the peptide may play a role through interactions with the CDR1. In this work we show that gp33 variants substituted at the peptidic termini at the putative CDR1 contact regions show improved recognition in B6 mice. The rank order of recognition is different using the P14 transgenic T cells, suggesting that one reason for improved recognition is a change in the TCR repertoire that recognizes the peptide. However, the affinity of the TCR by some of the peptide/MHC complex with increased recognition is improved, as shown by increased tetramer binding to P14 T cells. These substitutions at the termini of the peptide-binding cleft cause localized conformational changes as seen by changes in mAb binding and crystallographic structures. The different peptide structures also show different conformations in the center of the peptide, but these are shown to be energetically similar and thus most likely have no significance with respect to TCR recognition. Therefore, small conformational changes, localized to the CDR1 contact regions, may play a significant role in TCR recognition.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18271720 C.Bidot, F.Gruy, C.S.Haudin, F.El Hentati, B.Guy, and C.Lambert (2008).
Mathematical modeling of T-cell activation kinetic.
  J Comput Biol, 15, 105-128.  
17116886 J.Racape, F.Connan, J.Hoebeke, J.Choppin, and J.G.Guillet (2006).
Influence of dominant HIV-1 epitopes on HLA-A3/peptide complex formation.
  Proc Natl Acad Sci U S A, 103, 18208-18213.  
15837811 J.L.Chen, G.Stewart-Jones, G.Bossi, N.M.Lissin, L.Wooldridge, E.M.Choi, G.Held, P.R.Dunbar, R.M.Esnouf, M.Sami, J.M.Boulter, P.Rizkallah, C.Renner, A.Sewell, P.A.van der Merwe, B.K.Jakobsen, G.Griffiths, E.Y.Jones, and V.Cerundolo (2005).
Structural and kinetic basis for heightened immunogenicity of T cell vaccines.
  J Exp Med, 201, 1243-1255.
PDB codes: 2bnq 2bnr 2bnu
15557346 M.J.Miley, I.Messaoudi, B.M.Metzner, Y.Wu, J.Nikolich-Zugich, and D.H.Fremont (2004).
Structural basis for the restoration of TCR recognition of an MHC allelic variant by peptide secondary anchor substitution.
  J Exp Med, 200, 1445-1454.
PDB codes: 1rjy 1rjz 1rk0 1rk1
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.

 

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