2ckb
From Proteopedia
(New page: 200px<br /><applet load="2ckb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ckb, resolution 3.0Å" /> '''STRUCTURE OF THE 2C/K...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2ckb.gif|left|200px]]<br /><applet load="2ckb" size=" | + | [[Image:2ckb.gif|left|200px]]<br /><applet load="2ckb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ckb, resolution 3.0Å" /> | caption="2ckb, resolution 3.0Å" /> | ||
'''STRUCTURE OF THE 2C/KB/DEV8 COMPLEX'''<br /> | '''STRUCTURE OF THE 2C/KB/DEV8 COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The T cell receptor (TCR) inherently has dual specificity. T cells must | + | The T cell receptor (TCR) inherently has dual specificity. T cells must recognize self-antigens in the thymus during maturation and then discriminate between foreign pathogens in the periphery. A molecular basis for this cross-reactivity is elucidated by the crystal structure of the alloreactive 2C TCR bound to self peptide-major histocompatibility complex (pMHC) antigen H-2Kb-dEV8 refined against anisotropic 3.0 angstrom resolution x-ray data. The interface between peptide and TCR exhibits extremely poor shape complementarity, and the TCR beta chain complementarity-determining region 3 (CDR3) has minimal interaction with the dEV8 peptide. Large conformational changes in three of the TCR CDR loops are induced upon binding, providing a mechanism of structural plasticity to accommodate a variety of different peptide antigens. Extensive TCR interaction with the pMHC alpha helices suggests a generalized orientation that is mediated by the Valpha domain of the TCR and rationalizes how TCRs can effectively "scan" different peptides bound within a large, low-affinity MHC structural framework for those that provide the slight additional kinetic stabilization required for signaling. |
==About this Structure== | ==About this Structure== | ||
| - | 2CKB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 2CKB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKB OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Degano, M.]] | [[Category: Degano, M.]] | ||
| - | [[Category: Garcia, K | + | [[Category: Garcia, K C.]] |
| - | [[Category: Wilson, I | + | [[Category: Wilson, I A.]] |
[[Category: major histocompatibility complex]] | [[Category: major histocompatibility complex]] | ||
[[Category: t cell antigen receptor]] | [[Category: t cell antigen receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:31 2008'' |
Revision as of 14:49, 21 February 2008
|
STRUCTURE OF THE 2C/KB/DEV8 COMPLEX
Overview
The T cell receptor (TCR) inherently has dual specificity. T cells must recognize self-antigens in the thymus during maturation and then discriminate between foreign pathogens in the periphery. A molecular basis for this cross-reactivity is elucidated by the crystal structure of the alloreactive 2C TCR bound to self peptide-major histocompatibility complex (pMHC) antigen H-2Kb-dEV8 refined against anisotropic 3.0 angstrom resolution x-ray data. The interface between peptide and TCR exhibits extremely poor shape complementarity, and the TCR beta chain complementarity-determining region 3 (CDR3) has minimal interaction with the dEV8 peptide. Large conformational changes in three of the TCR CDR loops are induced upon binding, providing a mechanism of structural plasticity to accommodate a variety of different peptide antigens. Extensive TCR interaction with the pMHC alpha helices suggests a generalized orientation that is mediated by the Valpha domain of the TCR and rationalizes how TCRs can effectively "scan" different peptides bound within a large, low-affinity MHC structural framework for those that provide the slight additional kinetic stabilization required for signaling.
About this Structure
2CKB is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen., Garcia KC, Degano M, Pease LR, Huang M, Peterson PA, Teyton L, Wilson IA, Science. 1998 Feb 20;279(5354):1166-72. PMID:9469799
Page seeded by OCA on Thu Feb 21 16:49:31 2008
