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[[Image:1dqt.gif|left|200px]]
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{{STRUCTURE_1dqt|  PDB=1dqt  |  SCENE=  }}
'''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)'''


==THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)==
<StructureSection load='1dqt' size='340' side='right'caption='[[1dqt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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>
</table>
== 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 ==
[[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/dq/1dqt_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=1dqt ConSurf].
<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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1DQT 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=1DQT OCA].
</div>
<div class="pdbe-citations 1dqt" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11052947 11052947]
*[[CTLA-4|CTLA-4]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Almo SC]]
[[Category: Almo, S C.]]
[[Category: Nathenson SG]]
[[Category: Nathenson, S G.]]
[[Category: Ostrov DA]]
[[Category: Ostrov, D A.]]
[[Category: Schwartz JC]]
[[Category: Schwartz, J C.]]
[[Category: Shi W]]
[[Category: Shi, W.]]
[[Category: Homodimer]]
[[Category: Immunoglobulin variable domain-like beta-sandwich]]
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