1bec

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:17, 23 October 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1bec.jpg|left|200px]]
 
-
{{Structure
+
==BETA CHAIN OF A T CELL ANTIGEN RECEPTOR==
-
|PDB= 1bec |SIZE=350|CAPTION= <scene name='initialview01'>1bec</scene>, resolution 1.7&Aring;
+
<StructureSection load='1bec' size='340' side='right'caption='[[1bec]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1bec]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BEC FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bec OCA], [https://pdbe.org/1bec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bec RCSB], [https://www.ebi.ac.uk/pdbsum/1bec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bec ProSAT]</span></td></tr>
-
}}
+
</table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/be/1bec_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bec ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
'''BETA CHAIN OF A T CELL ANTIGEN RECEPTOR'''
+
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<ref>PMID:7701320</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1bec" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1BEC is a [[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].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/7701320 7701320]
+
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Bentley GA]]
-
[[Category: Bentley, G A.]]
+
[[Category: Boulot G]]
-
[[Category: Boulot, G.]]
+
[[Category: Karjalainen K]]
-
[[Category: Karjalainen, K.]]
+
[[Category: Mariuzza RA]]
-
[[Category: Mariuzza, R A.]]
+
-
[[Category: t cell receptor]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:09:54 2008''
+

Current revision

BETA CHAIN OF A T CELL ANTIGEN RECEPTOR

PDB ID 1bec

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools