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2ol3
From Proteopedia
(New page: 200px<br /><applet load="2ol3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ol3, resolution 2.90Å" /> '''crystal structure of...) |
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| - | [[Image:2ol3.gif|left|200px]]<br /><applet load="2ol3" size=" | + | [[Image:2ol3.gif|left|200px]]<br /><applet load="2ol3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ol3, resolution 2.90Å" /> | caption="2ol3, resolution 2.90Å" /> | ||
'''crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule'''<br /> | '''crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OL3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2OL3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OL3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tcr-pmhc complex]] | [[Category: tcr-pmhc complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:32:35 2008'' |
Revision as of 13:32, 23 January 2008
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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 with as ligand. 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 Mar 15;. PMID:17363906
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