2p24
From Proteopedia
(New page: 200px<br /><applet load="2p24" size="350" color="white" frame="true" align="right" spinBox="true" caption="2p24, resolution 2.15Å" /> '''I-Au/MBP125-135'''<b...) |
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==Overview== | ==Overview== | ||
| - | We report crystal structures of a negatively selected T cell receptor | + | We report crystal structures of a negatively selected T cell receptor (TCR) that recognizes two I-A(u)-restricted myelin basic protein peptides and one of its peptide/major histocompatibility complex (pMHC) ligands. Unusual complementarity-determining region (CDR) structural features revealed by our analyses identify a previously unrecognized mechanism by which the highly variable CDR3 regions define ligand specificity. In addition to the pMHC contact residues contributed by CDR3, the CDR3 residues buried deep within the V alpha/V beta interface exert indirect effects on recognition by influencing the V alpha/V beta interdomain angle. This phenomenon represents an additional mechanism for increasing the potential diversity of the TCR repertoire. Both the direct and indirect effects exerted by CDR residues can impact global TCR/MHC docking. Analysis of the available TCR structures in light of these results highlights the significance of the V alpha/V beta interdomain angle in determining specificity and indicates that TCR/pMHC interface features do not distinguish autoimmune from non-autoimmune class II-restricted TCRs. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: McBeth, C.]] | [[Category: McBeth, C.]] | ||
| - | [[Category: Strong, R | + | [[Category: Strong, R K.]] |
[[Category: i-au]] | [[Category: i-au]] | ||
[[Category: immune system]] | [[Category: immune system]] | ||
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[[Category: mhc]] | [[Category: mhc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:00 2008'' |
Revision as of 16:25, 21 February 2008
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I-Au/MBP125-135
Overview
We report crystal structures of a negatively selected T cell receptor (TCR) that recognizes two I-A(u)-restricted myelin basic protein peptides and one of its peptide/major histocompatibility complex (pMHC) ligands. Unusual complementarity-determining region (CDR) structural features revealed by our analyses identify a previously unrecognized mechanism by which the highly variable CDR3 regions define ligand specificity. In addition to the pMHC contact residues contributed by CDR3, the CDR3 residues buried deep within the V alpha/V beta interface exert indirect effects on recognition by influencing the V alpha/V beta interdomain angle. This phenomenon represents an additional mechanism for increasing the potential diversity of the TCR repertoire. Both the direct and indirect effects exerted by CDR residues can impact global TCR/MHC docking. Analysis of the available TCR structures in light of these results highlights the significance of the V alpha/V beta interdomain angle in determining specificity and indicates that TCR/pMHC interface features do not distinguish autoimmune from non-autoimmune class II-restricted TCRs.
About this Structure
2P24 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
A new twist in TCR diversity revealed by a forbidden alphabeta TCR., McBeth C, Seamons A, Pizarro JC, Fleishman SJ, Baker D, Kortemme T, Goverman JM, Strong RK, J Mol Biol. 2008 Feb 1;375(5):1306-19. Epub 2007 Nov 17. PMID:18155234
Page seeded by OCA on Thu Feb 21 18:25:00 2008
Categories: Mus musculus | Protein complex | McBeth, C. | Strong, R K. | I-au | Immune system | Immunoglobulin fold | Mbp | Mhc
