1i9e: Difference between revisions

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-[[Image:1i9e.jpg|left|200px]]<br /><applet load="1i9e" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1i9e, resolution 2.50&Aring;" />
-'''TCR DOMAIN'''<br />
-==Overview==
+==TCR DOMAIN==
-The T-cell receptor (TCR) is a heterodimeric cell-surface protein, consisting of two chains, alpha and beta, each of which is composed of a, variable (V) and a constant (C) domain. Crystals of the isolated V(alpha), domain of the murine TCR 2C were grown by serendipity from a solution, containing the extracellular domains of the intact TCR 2C and CD3 gamma, epsilon-chains. The V(alpha) crystal structure shows how crystal packing, can substitute for another V(alpha) domain in a different fashion from, that observed in V(alpha)/V(alpha) homodimer and V(alpha)/V(beta), heterodimer structures. Significant conformational changes occur in the, CDR3 and beta(3)beta(4) loops that normally form part of the dimer, interface. The monomeric V(alpha) domain provides the unique opportunity, to study the effect of dimerization on the conformation of the unliganded, complementarity-determining regions (CDR) of a TCR. This structure of an, individual V(alpha) module has implications for stability and, bioengineering of isolated antibody and immunoglobulin domains.
+<StructureSection load='1i9e' size='340' side='right'caption='[[1i9e]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1i9e]] 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=1I9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I9E FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9e OCA], [https://pdbe.org/1i9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9e RCSB], [https://www.ebi.ac.uk/pdbsum/1i9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9e ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TVA1_MOUSE TVA1_MOUSE]
+== 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/i9/1i9e_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=1i9e ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The T-cell receptor (TCR) is a heterodimeric cell-surface protein consisting of two chains, alpha and beta, each of which is composed of a variable (V) and a constant (C) domain. Crystals of the isolated V(alpha) domain of the murine TCR 2C were grown by serendipity from a solution containing the extracellular domains of the intact TCR 2C and CD3 gamma epsilon-chains. The V(alpha) crystal structure shows how crystal packing can substitute for another V(alpha) domain in a different fashion from that observed in V(alpha)/V(alpha) homodimer and V(alpha)/V(beta) heterodimer structures. Significant conformational changes occur in the CDR3 and beta(3)beta(4) loops that normally form part of the dimer interface. The monomeric V(alpha) domain provides the unique opportunity to study the effect of dimerization on the conformation of the unliganded complementarity-determining regions (CDR) of a TCR. This structure of an individual V(alpha) module has implications for stability and bioengineering of isolated antibody and immunoglobulin domains.
-==About this Structure==
+Crystal structure of an isolated V(alpha) domain of the 2C T-cell receptor.,Rudolph MG, Huang M, Teyton L, Wilson IA J Mol Biol. 2001 Nov 16;314(1):1-8. PMID:11724527<ref>PMID:11724527</ref>
-I9E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I9E OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure of an isolated V(alpha) domain of the 2C T-cell receptor., Rudolph MG, Huang M, Teyton L, Wilson IA, J Mol Biol. 2001 Nov 16;314(1):1-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11724527 11724527]
+</div>
+<div class="pdbe-citations 1i9e" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Huang M]]
-[[Category: Huang, M.]]
+[[Category: Rudolph MG]]
-[[Category: Rudolph, M.G.]]
+[[Category: Teyton L]]
-[[Category: Teyton, L.]]
+[[Category: Wilson IA]]
-[[Category: Wilson, I.A.]]
-[[Category: NAG]]
-[[Category: ig-like domain]]
-[[Category: t cell receptor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:11:52 2007''