1kb5
From Proteopedia
(New page: 200px<br /> <applet load="1kb5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kb5, resolution 2.5Å" /> '''MURINE T-CELL RECEPT...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1kb5.gif|left|200px]]<br /> | + | [[Image:1kb5.gif|left|200px]]<br /><applet load="1kb5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1kb5" size=" | + | |
caption="1kb5, resolution 2.5Å" /> | caption="1kb5, resolution 2.5Å" /> | ||
'''MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX'''<br /> | '''MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a mouse T-cell antigen receptor (TCR) Fv fragment | + | 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== | ==About this Structure== | ||
| - | 1KB5 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:// | + | 1KB5 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=1KB5 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Fontecilla-Camps, J | + | [[Category: Fontecilla-Camps, J C.]] |
[[Category: Gregoire, C.]] | [[Category: Gregoire, C.]] | ||
[[Category: Housset, D.]] | [[Category: Housset, D.]] | ||
| Line 26: | Line 25: | ||
[[Category: t-cell receptor]] | [[Category: t-cell receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:08 2008'' |
Revision as of 11:32, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 13:32:08 2008
