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PDBsum entry 2arj
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protein Protein-protein interface(s) links
Immune system PDB id
2arj

 

 

 

 

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Contents
Protein chains
211 a.a. *
212 a.a. *
116 a.a. *
Waters ×12
* Residue conservation analysis
PDB id:
2arj
Name: Immune system
Title: Cd8alpha-alpha in complex with yts 105.18 fab
Structure: Yts 105.18 antigen binding region light chain. Chain: l, a. Fragment: yts 105.18 fab light chain. Yts 105.18 antigen binding region heavy chain. Chain: h, b. Fragment: yts 105.18 fab heavy chain. T-cell surface glycoprotein cd8 alpha chain. Chain: r, q. Fragment: cd8alpha-alpha.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Strain: y3 myeloma. Cell_line: hybridoma. Mus musculus. House mouse. Organism_taxid: 10090. Gene: cd8a, lyt-2, lyt2.
Biol. unit: Hexamer (from PQS)
Resolution:
2.88Å     R-factor:   0.223     R-free:   0.277
Authors: D.A.Shore,L.Teyton,R.A.Dwek,P.M.Rudd,I.A.Wilson
Key ref:
D.A.Shore et al. (2006). Crystal structure of the TCR co-receptor CD8alphaalpha in complex with monoclonal antibody YTS 105.18 Fab fragment at 2.88 A resolution. J Mol Biol, 358, 347-354. PubMed id: 16530222 DOI: 10.1016/j.jmb.2006.02.016
Date:
19-Aug-05     Release date:   30-May-06    
PROCHECK
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 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 211 a.a.
Protein chains
No UniProt id for this chain
Struc: 212 a.a.
Protein chains
Pfam   ArchSchema ?
P01731  (CD8A_MOUSE) -  T-cell surface glycoprotein CD8 alpha chain from Mus musculus
Seq:
Struc: 		247 a.a.
116 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.jmb.2006.02.016 J Mol Biol 358:347-354 (2006)
PubMed id: 16530222  
 
 
Crystal structure of the TCR co-receptor CD8alphaalpha in complex with monoclonal antibody YTS 105.18 Fab fragment at 2.88 A resolution.
D.A.Shore, L.Teyton, R.A.Dwek, P.M.Rudd, I.A.Wilson.
 
  ABSTRACT  
 
The CD8 glycoprotein functions as an essential element in the control of T-cell selection, maturation and the TCR-mediated response to peptide antigen. CD8 is expressed as both heterodimeric CD8alphabeta and homodimeric CD8alphaalpha isoforms, which have distinct physiological roles and exhibit tissue-specific expression patterns. CD8alphaalpha has previously been crystallized in complex with class I pMHC and, more recently, with the mouse class Ib thymic leukemia antigen (TL). Here, we present the crystal structure of a soluble form of mouse CD8alphaalpha in complex with rat monoclonal antibody YTS 105.18 Fab fragment at 2.88 A resolution. YTS 105.18, which is commonly used in the blockade of CD8+ T-cell activation in response to peptide antigen, is specific for mouse CD8alpha. The YTS 105.18 Fab is one of only five rat IgG Fab structures to have been reported to date. Analysis of the YTS 105.18 Fab epitope on CD8alpha reveals that this antibody blocks CD8 activity by hydrogen bonding to residues that are critical for interaction with both class I pMHC and TL. Structural comparison of the liganded and unliganded forms of soluble CD8alphaalpha indicates that the mouse CD8alphaalpha immunoglobulin-domain dimer does not undergo significant structural alteration upon interaction either with class I pMHC or TL.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Mouse CD8aa complex with the YTS 105.18 Fab. (a) Ribbon diagram of the refined model of the CD8aa/YTS 105.18 Fab complex. Fab1 and Fab2 are in green and blue, respectively. The CD8a1 and CD8a2 subunits are in maroon. (b) The epitope for the YTS 105.18 Fab on the surface of the CD8aa subunit. YTS 105.18 binds the A, A' and B strands of CD8a. The epitope molecular surface (grey) covered by YTS 105.18 is superimposed on the ribbon diagram of CD8aa. Arg8 and Glu6 of CD8a, which are involved in hydrogen bonding to class I pMHC, TL and also to YTS 105.18 Fab, are indicated. The single N-glycosylation site at Asn42 within the CD8 construct is also indicated. 		Figure 3.
Figure 3. Comparison of CD8a interaction with YTS 105.18, H-2Kb and TL. (a) Expanded view of the interface between CD8a and YTS 105.18 Fab in stereo. The CD8aa/Fab complex is orientated as in Figure 1(a), with CD8a1 (maroon) on the left and YTS 105.18 Fab1 (blue) on the right. Hydrogen bonds are indicated by a broken line. (b) Equivalent stereo view of the interaction of CD8a1 (maroon) with class I pMHC (green), as defined in the CD8aa/H-2Kb complex structure.18 (c) Equivalent stereo view of the interaction between CD8a1 (maroon) and TL (purple), as defined in the CD8aa/TL complex structure.19
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2006, 358, 347-354) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19624124 A.M.Davis, and J.M.Berg (2009).
Homodimerization and heterodimerization of minimal zinc(II)-binding-domain peptides of T-cell proteins CD4, CD8alpha, and Lck.
  J Am Chem Soc, 131, 11492-11497.  
18929574 D.A.Shore, H.Issafras, E.Landais, L.Teyton, and I.A.Wilson (2008).
The crystal structure of CD8 in complex with YTS156.7.7 Fab and interaction with other CD8 antibodies define the binding mode of CD8 alphabeta to MHC class I.
  J Mol Biol, 384, 1190-1202.
PDB code: 3b9k
18074396 R.L.Rich, and D.G.Myszka (2007).
Survey of the year 2006 commercial optical biosensor literature.
  J Mol Recognit, 20, 300-366.  
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.

 

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