spacer
spacer

PDBsum entry 3e2h

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Immune system PDB id
3e2h

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
175 a.a. *
109 a.a. *
110 a.a. *
Ligands
GLN-LEU-SER-PRO-
PHE-PRO-PHE-ASP-
LEU
* Residue conservation analysis
PDB id:
3e2h
Name: Immune system
Title: Structure of the m67 high-affinity mutant of the 2c tcr in complex with ld/ql9
Structure: H-2 class i histocompatibility antigen, l-d alpha chain. Chain: a. Engineered: yes. Mutation: yes. Ql9 peptide. Chain: q. Engineered: yes. T-cell receptor alpha chain v region phds58. Chain: b.
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: h2-l. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this sequence occurs naturally in mouse.
Resolution:
3.80Å     R-factor:   0.223     R-free:   0.276
Authors: L.A.Colf,K.C.Garcia
Key ref: L.L.Jones et al. (2008). Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation. J Immunol, 181, 6255-6264. PubMed id: 18941216
Date:
05-Aug-08     Release date:   04-Nov-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01897  (HA1L_MOUSE) -  H-2 class I histocompatibility antigen, L-D alpha chain from Mus musculus
Seq:
Struc:
362 a.a.
175 a.a.*
Protein chain
Pfam   ArchSchema ?
P01738  (TVA1_MOUSE) -  T-cell receptor alpha chain V region PHDS58 from Mus musculus
Seq:
Struc:
130 a.a.
109 a.a.*
Protein chain
Pfam   ArchSchema ?
A2NTY6  (A2NTY6_MOUSE) -  Beta-chain (Fragment) from Mus musculus
Seq:
Struc:
144 a.a.
110 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 25 residue positions (black crosses)

 

 
J Immunol 181:6255-6264 (2008)
PubMed id: 18941216  
 
 
Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation.
L.L.Jones, L.A.Colf, J.D.Stone, K.C.Garcia, D.M.Kranz.
 
  ABSTRACT  
 
T cells are known to cross-react with diverse peptide MHC Ags through their alphabeta TCR. To explore the basis of such cross-reactivity, we examined the 2C TCR that recognizes two structurally distinct ligands, SIY-K(b) and alloantigen QL9-L(d). In this study we characterized the cross-reactivity of several high-affinity 2C TCR variants that contained mutations only in the CDR3alpha loop. Two of the TCR lost their ability to cross-react with the reciprocal ligand (SIY-K(b)), whereas another TCR (m67) maintained reactivity with both ligands. Crystal structures of four of the TCRs in complex with QL9-L(d) showed that CDR1, CDR2, and CDR3beta conformations and docking orientations were remarkably similar. Although the CDR3alpha loop of TCR m67 conferred a 2000-fold higher affinity for SIY-K(b), the TCR maintained the same docking angle on QL9-L(d) as the 2C TCR. Thus, CDR3alpha dictated the affinity and level of cross-reactivity, yet it did so without affecting the conserved docking orientation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20017116 R.L.Rich, and D.G.Myszka (2010).
Grading the commercial optical biosensor literature-Class of 2008: 'The Mighty Binders'.
  J Mol Recognit, 23, 1.  
19553539 A.S.Chervin, J.D.Stone, P.D.Holler, A.Bai, J.Chen, H.N.Eisen, and D.M.Kranz (2009).
The impact of TCR-binding properties and antigen presentation format on T cell responsiveness.
  J Immunol, 183, 1166-1178.  
19125887 J.D.Stone, A.S.Chervin, and D.M.Kranz (2009).
T-cell receptor binding affinities and kinetics: impact on T-cell activity and specificity.
  Immunology, 126, 165-176.  
19148199 K.C.Garcia, J.J.Adams, D.Feng, and L.K.Ely (2009).
The molecular basis of TCR germline bias for MHC is surprisingly simple.
  Nat Immunol, 10, 143-147.  
19416894 K.Rubtsova, J.P.Scott-Browne, F.Crawford, S.Dai, P.Marrack, and J.W.Kappler (2009).
Many different Vbeta CDR3s can reveal the inherent MHC reactivity of germline-encoded TCR V regions.
  Proc Natl Acad Sci U S A, 106, 7951-7956.  
19755422 N.A.Bowerman, L.A.Colf, K.C.Garcia, and D.M.Kranz (2009).
Different strategies adopted by K(b) and L(d) to generate T cell specificity directed against their respective bound peptides.
  J Biol Chem, 284, 32551-32561.  
19524428 S.J.Turner, N.L.La Gruta, K.Kedzierska, P.G.Thomas, and P.C.Doherty (2009).
Functional implications of T cell receptor diversity.
  Curr Opin Immunol, 21, 286-290.  
18973345 L.L.Jones, L.A.Colf, A.J.Bankovich, J.D.Stone, Y.G.Gao, C.M.Chan, R.H.Huang, K.C.Garcia, and D.M.Kranz (2008).
Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors.
  Biochemistry, 47, 12398-12408.
PDB code: 3ery
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.

 

spacer

spacer