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1dqt
From Proteopedia
(Difference between revisions)
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<StructureSection load='1dqt' size='340' side='right'caption='[[1dqt]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1dqt' size='340' side='right'caption='[[1dqt]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dqt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1dqt]] is a 4 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=1DQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=1dqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqt OCA], [https://pdbe.org/1dqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqt RCSB], [https://www.ebi.ac.uk/pdbsum/1dqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqt ProSAT]</span></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=1dqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqt OCA], [https://pdbe.org/1dqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqt RCSB], [https://www.ebi.ac.uk/pdbsum/1dqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/CTLA4_MOUSE CTLA4_MOUSE] Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28 (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1dqt ConSurf]. | </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=1dqt ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The effective regulation of T cell responses is dependent on opposing signals transmitted through two related cell-surface receptors, CD28 and cytotoxic T lymphocyte-associated antigen 4 (CTLA-4). Dimerization of CTLA-4 is required for the formation of high-avidity complexes with B7 ligands and for transmission of signals that attenuate T cell activation. We determined the crystal structure of the extracellular portion of CTLA-4 to 2.0 angstrom resolution. CTLA-4 belongs to the immunoglobulin superfamily and displays a strand topology similar to Valpha domains, with an unusual mode of dimerization that places the B7 binding sites distal to the dimerization interface. This organization allows each CTLA-4 dimer to bind two bivalent B7 molecules and suggests that a periodic arrangement of these components within the immunological synapse may contribute to the regulation of T cell responsiveness. | ||
| - | |||
| - | Structure of murine CTLA-4 and its role in modulating T cell responsiveness.,Ostrov DA, Shi W, Schwartz JC, Almo SC, Nathenson SG Science. 2000 Oct 27;290(5492):816-9. PMID:11052947<ref>PMID:11052947</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dqt" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[CTLA-4|CTLA-4]] | *[[CTLA-4|CTLA-4]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Almo | + | [[Category: Almo SC]] |
| - | [[Category: Nathenson | + | [[Category: Nathenson SG]] |
| - | [[Category: Ostrov | + | [[Category: Ostrov DA]] |
| - | [[Category: Schwartz | + | [[Category: Schwartz JC]] |
| - | [[Category: Shi | + | [[Category: Shi W]] |
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| - | + | ||
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Current revision
THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)
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