1yjd: Difference between revisions
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New page: left|200px<br /> <applet load="1yjd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yjd, resolution 2.700Å" /> '''Crystal structure ... |
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== | ==Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)== | ||
Naive T cell activation requires signaling by the T cell receptor and by | <StructureSection load='1yjd' size='340' side='right'caption='[[1yjd]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1yjd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YJD 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]] 2.7Å</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=1yjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjd OCA], [https://pdbe.org/1yjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yjd RCSB], [https://www.ebi.ac.uk/pdbsum/1yjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yjd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CD28_HUMAN CD28_HUMAN] Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival. | |||
== 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/yj/1yjd_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=1yjd ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Naive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. Structural comparisons redefine the evolutionary relationships of CD28-related proteins, antigen receptors and adhesion molecules and account for the distinct ligand-binding and stoichiometric properties of CD28 and the related, inhibitory homodimer CTLA-4. Cryo-electron microscopy-based comparisons of complexes of CD28 with mitogenic and nonmitogenic antibodies place new constraints on models of antibody-induced receptor triggering. This work completes the initial structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system. | |||
Crystal structure of a soluble CD28-Fab complex.,Evans EJ, Esnouf RM, Manso-Sancho R, Gilbert RJ, James JR, Yu C, Fennelly JA, Vowles C, Hanke T, Walse B, Hunig T, Sorensen P, Stuart DI, Davis SJ Nat Immunol. 2005 Mar;6(3):271-9. Epub 2005 Feb 6. PMID:15696168<ref>PMID:15696168</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1yjd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[3D structures of non-human antibody|3D structures of non-human antibody]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Davis SJ]] | |||
[[Category: Davis | [[Category: Esnouf RM]] | ||
[[Category: Esnouf | [[Category: Evans EJ]] | ||
[[Category: Evans | [[Category: Gilbert RJC]] | ||
[[Category: Gilbert | [[Category: James JR]] | ||
[[Category: James | [[Category: Manso-Sancho R]] | ||
[[Category: Manso-Sancho | [[Category: Sorensen P]] | ||
[[Category: Sorensen | [[Category: Stuart DI]] | ||
[[Category: Stuart | |||
Latest revision as of 08:03, 15 May 2024
Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)
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