1bec
From Proteopedia
(New page: 200px<br /><applet load="1bec" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bec, resolution 1.7Å" /> '''BETA CHAIN OF A T CEL...) |
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| - | [[Image:1bec.jpg|left|200px]]<br /><applet load="1bec" size=" | + | [[Image:1bec.jpg|left|200px]]<br /><applet load="1bec" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bec, resolution 1.7Å" /> | caption="1bec, resolution 1.7Å" /> | ||
'''BETA CHAIN OF A T CELL ANTIGEN RECEPTOR'''<br /> | '''BETA CHAIN OF A T CELL ANTIGEN RECEPTOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the extracellular portion of the beta chain of a | + | The crystal structure of the extracellular portion of the beta chain of a murine T cell antigen receptor (TCR), determined at a resolution of 1.7 angstroms, shows structural homology to immunoglobulins. The structure of the first and second hypervariable loops suggested that, in general, they adopt more restricted sets of conformations in TCR beta chains than those found in immunoglobulins; the third hypervariable loop had certain structural characteristics in common with those of immunoglobulin heavy chain variable domains. The variable and constant domains were in close contact, presumably restricting the flexibility of the beta chain. This may facilitate signal transduction from the TCR to the associated CD3 molecules in the TCR-CD3 complex. |
==About this Structure== | ==About this Structure== | ||
| - | 1BEC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1BEC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1BEC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bentley, G | + | [[Category: Bentley, G A.]] |
[[Category: Boulot, G.]] | [[Category: Boulot, G.]] | ||
[[Category: Karjalainen, K.]] | [[Category: Karjalainen, K.]] | ||
| - | [[Category: Mariuzza, R | + | [[Category: Mariuzza, R A.]] |
[[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 11:54:23 2008'' |
Revision as of 09:54, 21 February 2008
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BETA CHAIN OF A T CELL ANTIGEN RECEPTOR
Overview
The crystal structure of the extracellular portion of the beta chain of a murine T cell antigen receptor (TCR), determined at a resolution of 1.7 angstroms, shows structural homology to immunoglobulins. The structure of the first and second hypervariable loops suggested that, in general, they adopt more restricted sets of conformations in TCR beta chains than those found in immunoglobulins; the third hypervariable loop had certain structural characteristics in common with those of immunoglobulin heavy chain variable domains. The variable and constant domains were in close contact, presumably restricting the flexibility of the beta chain. This may facilitate signal transduction from the TCR to the associated CD3 molecules in the TCR-CD3 complex.
About this Structure
1BEC is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the beta chain of a T cell antigen receptor., Bentley GA, Boulot G, Karjalainen K, Mariuzza RA, Science. 1995 Mar 31;267(5206):1984-7. PMID:7701320
Page seeded by OCA on Thu Feb 21 11:54:23 2008
