2ol3
From Proteopedia
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- | [[Image:2ol3.gif|left|200px]] | + | [[Image:2ol3.gif|left|200px]] |
- | + | ||
- | '''crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule''' | + | {{Structure |
+ | |PDB= 2ol3 |SIZE=350|CAPTION= <scene name='initialview01'>2ol3</scene>, resolution 2.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= B2m ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
+ | }} | ||
+ | |||
+ | '''crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2OL3 is a [ | + | 2OL3 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=2OL3 OCA]. |
==Reference== | ==Reference== | ||
- | How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?, Mazza C, Auphan-Anezin N, Gregoire C, Guimezanes A, Kellenberger C, Roussel A, Kearney A, van der Merwe PA, Schmitt-Verhulst AM, Malissen B, EMBO J. 2007 Apr 4;26(7):1972-83. Epub 2007 Mar 15. PMID:[http:// | + | How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?, Mazza C, Auphan-Anezin N, Gregoire C, Guimezanes A, Kellenberger C, Roussel A, Kearney A, van der Merwe PA, Schmitt-Verhulst AM, Malissen B, EMBO J. 2007 Apr 4;26(7):1972-83. Epub 2007 Mar 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17363906 17363906] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: tcr-pmhc complex]] | [[Category: tcr-pmhc complex]] | ||
- | ''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 18:01:07 2008'' |
Revision as of 16:01, 20 March 2008
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, resolution 2.90Å | |||||||
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Ligands: | |||||||
Gene: | B2m (Mus musculus) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule
Overview
Binding degeneracy is thought to constitute a fundamental property of the T-cell antigen receptor (TCR), yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and a peptide (pBM8) bound to the H-2K(bm8) major histocompatibility complex (MHC) molecule, and compared it with the structures of the BM3.3 TCR bound to H-2K(b) molecules loaded with two peptides that had a minimal level of primary sequence identity with pBM8. Our findings provide a refined structural view of the basis of BM3.3 TCR cross-reactivity and a structural explanation for the long-standing paradox that a TCR antigen-binding site can be both specific and degenerate. We also measured the thermodynamic features and biological penalties that incurred during cross-recognition. Our data illustrate the difficulty for a given TCR in adapting to distinct peptide-MHC surfaces while still maintaining affinities that result in functional in vivo responses. Therefore, when induction of protective effector T cells is used as the ultimate criteria for adaptive immunity, TCRs are probably much less degenerate than initially assumed.
About this Structure
2OL3 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?, Mazza C, Auphan-Anezin N, Gregoire C, Guimezanes A, Kellenberger C, Roussel A, Kearney A, van der Merwe PA, Schmitt-Verhulst AM, Malissen B, EMBO J. 2007 Apr 4;26(7):1972-83. Epub 2007 Mar 15. PMID:17363906
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