This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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 ...) |
|||
| Line 4: | Line 4: | ||
==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== | ||
| Line 13: | Line 13: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 18:59:46 2008
