PDBsum entry 1ac6

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protein Protein-protein interface(s) links
Receptor PDB id
Protein chains
110 a.a. *
Waters ×116
* Residue conservation analysis
PDB id:
Name: Receptor
Title: Crystal structure of a variable domain mutant of a t-cell re alpha chain
Structure: T-cell receptor alpha. Chain: a, b. Fragment: variable domain. Mutation: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090
2.30Å     R-factor:   0.161     R-free:   0.279
Authors: H.-M.Li,R.A.Mariuzza
Key ref:
H.Li et al. (1997). Dual conformations of a T cell receptor V alpha homodimer: implications for variability in V alpha V beta domain association. J Mol Biol, 269, 385-394. PubMed id: 9199407 DOI: 10.1006/jmbi.1997.1047
13-Feb-97     Release date:   25-Feb-98    
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Protein chains
Pfam   ArchSchema ?
Q5R1F5  (Q5R1F5_MOUSE) -  TRAV6D-7 (Fragment)
112 a.a.
110 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


DOI no: 10.1006/jmbi.1997.1047 J Mol Biol 269:385-394 (1997)
PubMed id: 9199407  
Dual conformations of a T cell receptor V alpha homodimer: implications for variability in V alpha V beta domain association.
H.Li, M.I.Lebedeva, E.S.Ward, R.A.Mariuzza.
The crystal structure of a mutant T cell receptor (TCR) V alpha domain containing a grafted third complementarity-determining region (CDR3) from a different V alpha was determined at 2.3 A resolution by molecular replacement using the wild-type V alpha structure as a search model. Like the wild-type V alpha domain, the mutant crystallized as a homodimer very similar to TCR V alpha V beta and antibody V(L)V(H) heterodimers, with the CDR loops disposed to form part of the antigen-binding site. However, the relative orientation of the two chains in the mutant V alpha homodimer differs from that in the wild-type by a rotation of 14 degrees such that the buried surface area in the dimer interface of the mutant is 140 A2 less than in the wild-type. While the residues forming the interface are essentially the same in the two structures, there are only four pairs of interface hydrogen bonds in the case of the mutant compared with eight for the wild-type. These results suggest that multiple relative orientations of the V alpha and V beta domains of TCRs may be possible, providing a significant contribution to TCR combining site diversity.
  Selected figure(s)  
Figure 2.
Figure 2. The 2 F[o]−F[c] electron density maps for 1934.4 Vα[mut] CDR loops. A, CDR1; B, CDR2 and C, CDR3 of monomer 1. D, CDR3 of monomer 2. Maps are contoured at 1 σ for CDR1 and CDR2 and at 0.6 σ for CDR3. Hydrogen bonds are dotted pink lines. Carbon, nitrogen and oxygen atoms are colored yellow, blue and red, respectively.
Figure 3.
Figure 3. Stereoview of VαVα dimers showing hydrogen bonds and water molecules in the domain interfaces of mutant (A) and wild-type (B) 1934.4 Vα structures. Monomers 1 and 2 are colored blue and yellow, respectively. Hydrogen bonds are dotted pink lines and water molecules are red spheres. Nitrogen and oxygen atoms are colored blue and red, respectively.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1997, 269, 385-394) copyright 1997.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
17694060 D.Feng, C.J.Bond, L.K.Ely, J.Maynard, and K.C.Garcia (2007).
Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'.
  Nat Immunol, 8, 975-983.
PDB codes: 2pxy 2z31 2z35
17449678 K.M.Armstrong, and B.M.Baker (2007).
A comprehensive calorimetric investigation of an entropically driven T cell receptor-peptide/major histocompatibility complex interaction.
  Biophys J, 93, 597-609.  
16551255 M.G.Rudolph, R.L.Stanfield, and I.A.Wilson (2006).
How TCRs bind MHCs, peptides, and coreceptors.
  Annu Rev Immunol, 24, 419-466.  
16260763 H.Li, S.Van Vranken, Y.Zhao, Z.Li, Y.Guo, L.Eisele, and Y.Li (2005).
Crystal structures of T cell receptor (beta) chains related to rheumatoid arthritis.
  Protein Sci, 14, 3025-3038.
PDB codes: 2axh 2axj
11988465 M.G.Rudolph, J.G.Luz, and I.A.Wilson (2002).
Structural and thermodynamic correlates of T cell signaling.
  Annu Rev Biophys Biomol Struct, 31, 121-149.  
10358763 K.C.Garcia, L.Teyton, and I.A.Wilson (1999).
Structural basis of T cell recognition.
  Annu Rev Immunol, 17, 369-397.  
9700511 G.Mazza, D.Housset, C.Piras, C.Gregoire, S.Y.Lin, J.C.Fontecilla-Camps, and B.Malissen (1998).
Glimpses at the recognition of peptide/MHC complexes by T-cell antigen receptors.
  Immunol Rev, 163, 187-196.  
9700510 H.Li, A.Llera, and R.A.Mariuzza (1998).
Structure-function studies of T-cell receptor-superantigen interactions.
  Immunol Rev, 163, 177-186.  
9824474 M.Feng, D.Chou, Y.Liaw, and M.Lai (1998).
Conserved T-cell receptor class II major histocompatibility complex contact detected in a T-lymphocyte population.
  Immunology, 95, 185-192.  
9434905 I.A.Wilson, and K.C.Garcia (1997).
T-cell receptor structure and TCR complexes.
  Curr Opin Struct Biol, 7, 839-848.  
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.