1kb5
From Proteopedia
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- | [[Image:1kb5.gif|left|200px]] | + | [[Image:1kb5.gif|left|200px]] |
- | + | ||
- | '''MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX''' | + | {{Structure |
+ | |PDB= 1kb5 |SIZE=350|CAPTION= <scene name='initialview01'>1kb5</scene>, resolution 2.5Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1KB5 is a [ | + | 1KB5 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=1KB5 OCA]. |
==Reference== | ==Reference== | ||
- | The three-dimensional structure of a T-cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the V beta domain., Housset D, Mazza G, Gregoire C, Piras C, Malissen B, Fontecilla-Camps JC, EMBO J. 1997 Jul 16;16(14):4205-16. PMID:[http:// | + | The three-dimensional structure of a T-cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the V beta domain., Housset D, Mazza G, Gregoire C, Piras C, Malissen B, Fontecilla-Camps JC, EMBO J. 1997 Jul 16;16(14):4205-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9250664 9250664] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: t-cell receptor]] | [[Category: t-cell 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 12:14:59 2008'' |
Revision as of 10:15, 20 March 2008
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, resolution 2.5Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX
Overview
The crystal structure of a mouse T-cell antigen receptor (TCR) Fv fragment complexed to the Fab fragment of a specific anti-clonotypic antibody has been determined to 2.6 A resolution. The polypeptide backbone of the TCR V alpha domain is very similar to those of other crystallographically determined V alphas, whereas the V beta structure is so far unique among TCR V beta domains in that it displays a switch of the c" strand from the inner to the outer beta-sheet. The beta chain variable region of this TCR antigen-binding site is characterized by a rather elongated third complementarity-determining region (CDR3beta) that packs tightly against the CDR3 loop of the alpha chain, without leaving any intervening hydrophobic pocket. Thus, the conformation of the CDR loops with the highest potential diversity distinguishes the structure of this TCR antigen-binding site from those for which crystallographic data are available. On the basis of all these results, we infer that a significant conformational change of the CDR3beta loop found in our TCR is required for binding to its cognate peptide-MHC ligand.
About this Structure
1KB5 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of a T-cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the V beta domain., Housset D, Mazza G, Gregoire C, Piras C, Malissen B, Fontecilla-Camps JC, EMBO J. 1997 Jul 16;16(14):4205-16. PMID:9250664
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