1fg2
From Proteopedia
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| - | [[Image:1fg2.gif|left|200px]] | + | [[Image:1fg2.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE LCMV PEPTIDIC EPITOPE GP33 IN COMPLEX WITH THE MURINE CLASS I MHC MOLECULE H-2DB''' | + | {{Structure |
| + | |PDB= 1fg2 |SIZE=350|CAPTION= <scene name='initialview01'>1fg2</scene>, resolution 2.754Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE LCMV PEPTIDIC EPITOPE GP33 IN COMPLEX WITH THE MURINE CLASS I MHC MOLECULE H-2DB''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FG2 is a [ | + | 1FG2 is a [[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== | ||
| - | Viral escape at the molecular level explained by quantitative T-cell receptor/peptide/MHC interactions and the crystal structure of a peptide/MHC complex., Tissot AC, Ciatto C, Mittl PR, Grutter MG, Pluckthun A, J Mol Biol. 2000 Sep 29;302(4):873-85. PMID:[http:// | + | Viral escape at the molecular level explained by quantitative T-cell receptor/peptide/MHC interactions and the crystal structure of a peptide/MHC complex., Tissot AC, Ciatto C, Mittl PR, Grutter MG, Pluckthun A, J Mol Biol. 2000 Sep 29;302(4):873-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10993729 10993729] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ig fold]] | [[Category: ig fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:08:39 2008'' |
Revision as of 09:08, 20 March 2008
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| , resolution 2.754Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE LCMV PEPTIDIC EPITOPE GP33 IN COMPLEX WITH THE MURINE CLASS I MHC MOLECULE H-2DB
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.
About this Structure
1FG2 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Viral escape at the molecular level explained by quantitative T-cell receptor/peptide/MHC interactions and the crystal structure of a peptide/MHC complex., Tissot AC, Ciatto C, Mittl PR, Grutter MG, Pluckthun A, J Mol Biol. 2000 Sep 29;302(4):873-85. PMID:10993729
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