2z35
From Proteopedia
(New page: 200px<br /><applet load="2z35" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z35, resolution 2.2Å" /> '''Crystal structure of ...) |
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==Overview== | ==Overview== | ||
| - | All complexes of T cell receptors (TCRs) bound to peptide-major | + | All complexes of T cell receptors (TCRs) bound to peptide-major histocompatibility complex (pMHC) molecules assume a stereotyped binding 'polarity', despite wide variations in TCR-pMHC docking angles. However, existing TCR-pMHC crystal structures have failed to show broadly conserved pairwise interaction motifs. Here we determined the crystal structures of two TCRs encoded by the variable beta-chain 8.2 (V(beta)8.2), each bound to the MHC class II molecule I-A(u), and did energetic mapping of V(alpha) and V(beta) contacts with I-A(u). Together with two previously solved structures of V(beta)8.2-containing TCR-MHC complexes, we found four TCR-I-A complexes with structurally superimposable interactions between the V(beta) loops and the I-A alpha-helix. This examination of a narrow 'slice' of the TCR-MHC repertoire demonstrates what is probably one of many germline-derived TCR-MHC interaction 'codons'. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bond, C | + | [[Category: Bond, C J.]] |
| - | [[Category: Ely, L | + | [[Category: Ely, L K.]] |
[[Category: Feng, D.]] | [[Category: Feng, D.]] | ||
| - | [[Category: Garcia, K | + | [[Category: Garcia, K C.]] |
[[Category: immune receptor]] | [[Category: immune receptor]] | ||
[[Category: immune system]] | [[Category: immune system]] | ||
| - | ''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 18:59:46 2008'' |
Revision as of 16:59, 21 February 2008
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Crystal structure of immune receptor
Overview
All complexes of T cell receptors (TCRs) bound to peptide-major histocompatibility complex (pMHC) molecules assume a stereotyped binding 'polarity', despite wide variations in TCR-pMHC docking angles. However, existing TCR-pMHC crystal structures have failed to show broadly conserved pairwise interaction motifs. Here we determined the crystal structures of two TCRs encoded by the variable beta-chain 8.2 (V(beta)8.2), each bound to the MHC class II molecule I-A(u), and did energetic mapping of V(alpha) and V(beta) contacts with I-A(u). Together with two previously solved structures of V(beta)8.2-containing TCR-MHC complexes, we found four TCR-I-A complexes with structurally superimposable interactions between the V(beta) loops and the I-A alpha-helix. This examination of a narrow 'slice' of the TCR-MHC repertoire demonstrates what is probably one of many germline-derived TCR-MHC interaction 'codons'.
About this Structure
2Z35 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'., Feng D, Bond CJ, Ely LK, Maynard J, Garcia KC, Nat Immunol. 2007 Sep;8(9):975-83. Epub 2007 Aug 12. PMID:17694060
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