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New page: left|200px<br /><applet load="1fg2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fg2, resolution 2.754Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1fg2.gif|left|200px]]<br /><applet load="1fg2" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fg2.gif|left|200px]]<br /><applet load="1fg2" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fg2, resolution 2.754&Aring;" />
caption="1fg2, resolution 2.754&Aring;" />
'''CRYSTAL STRUCTURE OF THE LCMV PEPTIDIC EPITOPE GP33 IN COMPLEX WITH THE MURINE CLASS I MHC MOLECULE H-2DB'''<br />
'''CRYSTAL STRUCTURE OF THE LCMV PEPTIDIC EPITOPE GP33 IN COMPLEX WITH THE MURINE CLASS I MHC MOLECULE H-2DB'''<br />


==Overview==
==Overview==
Viral escape, first characterized for the lymphocytic choriomeningitis, virus (LCMV) in a mouse transgenic for the P14 T cell-receptor (TCR), can, be due to mutations in T-cell epitopes. We have measured the affinity, between the H-2D(b) containing the wild-type and two of its "viral escape", epitopes, as well as other altered peptide ligands (APL), by using BIACORE, analysis, and solved the crystal structure of H-2D(b) in complex with the, wild-type peptide at 2.75 A resolution. We show that viral escape is due, to a 50 to 100-fold reduction in the level of affinity between the P14 TCR, and the binary complexes of the MHC molecule with the different peptides., Structurally, one of the mutations alters a TCR contact residue, while the, effect of the other on the binding of the TCR must be indirect through, structural rearrangements. The former is a null ligand, while the latter, still leads to some central tolerance. This work defines the structural, and energetic threshold for viral escape.
Viral escape, first characterized for the lymphocytic choriomeningitis virus (LCMV) in a mouse transgenic for the P14 T cell-receptor (TCR), can be due to mutations in T-cell epitopes. We have measured the affinity between the H-2D(b) containing the wild-type and two of its "viral escape" epitopes, as well as other altered peptide ligands (APL), by using BIACORE analysis, and solved the crystal structure of H-2D(b) in complex with the wild-type peptide at 2.75 A resolution. We show that viral escape is due to a 50 to 100-fold reduction in the level of affinity between the P14 TCR and the binary complexes of the MHC molecule with the different peptides. Structurally, one of the mutations alters a TCR contact residue, while the effect of the other on the binding of the TCR must be indirect through structural rearrangements. The former is a null ligand, while the latter still leads to some central tolerance. This work defines the structural and energetic threshold for viral escape.


==About this Structure==
==About this Structure==
1FG2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FG2 OCA].  
1FG2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FG2 OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Ciatto, C.]]
[[Category: Ciatto, C.]]
[[Category: Gruetter, M.G.]]
[[Category: Gruetter, M G.]]
[[Category: Mittl, P.R.E.]]
[[Category: Mittl, P R.E.]]
[[Category: Plueckthun, A.]]
[[Category: Plueckthun, A.]]
[[Category: Tissot, A.C.]]
[[Category: Tissot, A C.]]
[[Category: ig fold]]
[[Category: ig fold]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:17 2008''