2ol3: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= B2m ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= B2m ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ol3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ol3 OCA], [http://www.ebi.ac.uk/pdbsum/2ol3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ol3 RCSB]</span> | |||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: Roussel, A.]] | [[Category: Roussel, A.]] | ||
[[Category: Schmitt-Verhulst, A M.]] | [[Category: Schmitt-Verhulst, A M.]] | ||
[[Category: class i mhc]] | [[Category: class i mhc]] | ||
[[Category: h-2kbm8]] | [[Category: h-2kbm8]] | ||
| Line 38: | Line 40: | ||
[[Category: tcr-pmhc complex]] | [[Category: tcr-pmhc complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:19:23 2008'' | ||
Revision as of 04:19, 31 March 2008
| |||||||
| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | B2m (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule
OverviewOverview
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 StructureAbout this Structure
2OL3 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Mon Mar 31 04:19:23 2008