This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1dqt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:52, 20 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dqt.gif|left|200px]]
 
-
{{Structure
+
==THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)==
-
|PDB= 1dqt |SIZE=350|CAPTION= <scene name='initialview01'>1dqt</scene>, resolution 2.0&Aring;
+
<StructureSection load='1dqt' size='340' side='right'caption='[[1dqt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
+
<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>
-
|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]] 2&#8491;</td></tr>
-
|GENE=
+
<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/initialview01.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>
-
'''THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)'''
+
==See Also==
-
 
+
*[[CTLA-4|CTLA-4]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
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.
+
[[Category: Large Structures]]
-
 
+
-
==About this Structure==
+
-
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].
+
-
 
+
-
==Reference==
+
-
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]
+
[[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: CL]]
+
-
[[Category: EDO]]
+
-
[[Category: homodimer]]
+
-
[[Category: immunoglobulin variable domain-like beta-sandwich]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:52 2008''
+

Current revision

THE CRYSTAL STRUCTURE OF MURINE CTLA4 (CD152)

PDB ID 1dqt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dqt"
Personal tools