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1i85

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[[Image:1i85.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE CTLA-4/B7-2 COMPLEX==
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The line below this paragraph, containing "STRUCTURE_1i85", creates the "Structure Box" on the page.
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<StructureSection load='1i85' size='340' side='right'caption='[[1i85]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1i85]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I85 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i85 OCA], [https://pdbe.org/1i85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i85 RCSB], [https://www.ebi.ac.uk/pdbsum/1i85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i85 ProSAT]</span></td></tr>
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{{STRUCTURE_1i85| PDB=1i85 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CD86_HUMAN CD86_HUMAN] Receptor involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. May play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T-cells within 24 hours after activation. Isoform 2 interferes with the formation of CD86 clusters, and thus acts as a negative regulator of T-cell activation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i8/1i85_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1i85 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF THE CTLA-4/B7-2 COMPLEX'''
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==See Also==
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*[[CTLA-4|CTLA-4]]
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__TOC__
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==Overview==
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</StructureSection>
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Regulation of T-cell activity is dependent on antigen-independent co-stimulatory signals provided by the disulphide-linked homodimeric T-cell surface receptors, CD28 and CTLA-4 (ref. 1). Engagement of CD28 with B7-1 and B7-2 ligands on antigen-presenting cells (APCs) provides a stimulatory signal for T-cell activation, whereas subsequent engagement of CTLA-4 with these same ligands results in attenuation of the response. Given their central function in immune modulation, CTLA-4- and CD28-associated signalling pathways are primary therapeutic targets for preventing autoimmune disease, graft versus host disease, graft rejection and promoting tumour immunity. However, little is known about the cell-surface organization of these receptor/ligand complexes and the structural basis for signal transduction. Here we report the 3.2-A resolution structure of the complex between the disulphide-linked homodimer of human CTLA-4 and the receptor-binding domain of human B7-2. The unusual dimerization properties of both CTLA-4 and B7-2 place their respective ligand-binding sites distal to the dimer interface in each molecule and promote the formation of an alternating arrangement of bivalent CTLA-4 and B7-2 dimers that extends throughout the crystal. Direct observation of this CTLA-4/B7-2 network provides a model for the periodic organization of these molecules within the immunological synapse and suggests a distinct mechanism for signalling by dimeric cell-surface receptors.
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==Disease==
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Known disease associated with this structure: Celiac disease, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=123890 123890]], Diabetes mellitus, insulin-dependent, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=123890 123890]], Graves disease, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=123890 123890]], Hypothyroidism, autoimmune OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=123890 123890]]
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==About this Structure==
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1I85 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I85 OCA].
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==Reference==
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Structural basis for co-stimulation by the human CTLA-4/B7-2 complex., Schwartz JC, Zhang X, Fedorov AA, Nathenson SG, Almo SC, Nature. 2001 Mar 29;410(6828):604-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11279501 11279501]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Almo, S C.]]
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[[Category: Almo SC]]
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[[Category: Fedorov, A A.]]
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[[Category: Fedorov AA]]
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[[Category: Nathenson, S G.]]
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[[Category: Nathenson SG]]
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[[Category: Schwartz, J C.D.]]
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[[Category: Schwartz J-CD]]
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[[Category: Zhang, X.]]
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[[Category: Zhang X]]
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[[Category: Ig v-type domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:41:38 2008''
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Current revision

CRYSTAL STRUCTURE OF THE CTLA-4/B7-2 COMPLEX

PDB ID 1i85

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