2ckb
From Proteopedia
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| - | [[Image:2ckb.gif|left|200px]] | + | [[Image:2ckb.gif|left|200px]] |
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| - | '''STRUCTURE OF THE 2C/KB/DEV8 COMPLEX''' | + | {{Structure |
| + | |PDB= 2ckb |SIZE=350|CAPTION= <scene name='initialview01'>2ckb</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE OF THE 2C/KB/DEV8 COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CKB is a [ | + | 2CKB is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9469799 9469799] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: t cell antigen receptor]] | [[Category: t cell antigen receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:27 2008'' |
Revision as of 14:16, 20 March 2008
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| , resolution 3.0Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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