3b9i
From Proteopedia
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(New page: 200px<br /><applet load="3b9i" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b9i, resolution 2.490Å" /> '''Crystal Structure o...) |
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| - | [[Image:3b9i.jpg|left|200px]]<br /><applet load="3b9i" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="3b9i, resolution 2.490Å" /> | ||
| - | '''Crystal Structure of mouse GITRL at 2.5 A.'''<br /> | ||
| - | == | + | ==Crystal Structure of mouse GITRL at 2.5 A.== |
| - | + | <StructureSection load='3b9i' size='340' side='right'caption='[[3b9i]], [[Resolution|resolution]] 2.49Å' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[3b9i]] is a 2 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=3B9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B9I 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]] 2.49Å</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=3b9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9i OCA], [https://pdbe.org/3b9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b9i RCSB], [https://www.ebi.ac.uk/pdbsum/3b9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9i ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/TNF18_MOUSE TNF18_MOUSE] Cytokine that binds to TNFRSF18/AITR/GITR (PubMed:14521928, PubMed:14647196). Regulates T-cell responses (PubMed:14647196). Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation (PubMed:14608036, PubMed:15128759). Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B (PubMed:14521928, PubMed:14647196, PubMed:18178614). Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1 (By similarity). Promotes leukocyte adhesion to endothelial cells (PubMed:23892569). Regulates migration of monocytes from the splenic reservoir to sites of inflammation (PubMed:24107315).[UniProtKB:Q9UNG2]<ref>PMID:14521928</ref> <ref>PMID:14608036</ref> <ref>PMID:14647196</ref> <ref>PMID:15128759</ref> <ref>PMID:18178614</ref> <ref>PMID:23892569</ref> <ref>PMID:24107315</ref> |
| - | [[ | + | == 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/b9/3b9i_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=3b9i ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glucocorticoid-induced TNF receptor ligand (GITRL), a recently identified member of the TNF superfamily, binds to its receptor, GITR, on both effector and regulatory T cells and generates positive costimulatory signals implicated in a wide range of T cell functions. In contrast to all previously characterized homotrimeric TNF family members, the mouse GITRL crystal structure reveals a previously unrecognized dimeric assembly that is stabilized via a unique "domain-swapping" interaction. Consistent with its crystal structure, mouse GITRL exists as a stable dimer in solution. Structure-guided mutagenesis studies confirmed the determinants responsible for dimerization and support a previously unrecognized receptor-recognition surface for mouse GITRL that has not been observed for any other TNF family members. Taken together, the unique structural and biochemical behavior of mouse GITRL, along with the unusual domain organization of murine GITR, support a previously unrecognized mechanism for signaling within the TNF superfamily. | ||
| - | + | Evolution of GITRL immune function: murine GITRL exhibits unique structural and biochemical properties within the TNF superfamily.,Chattopadhyay K, Ramagopal UA, Brenowitz M, Nathenson SG, Almo SC Proc Natl Acad Sci U S A. 2008 Jan 15;105(2):635-40. Epub 2008 Jan 8. PMID:18182486<ref>PMID:18182486</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3b9i" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Tumor necrosis factor ligand superfamily 3D structures|Tumor necrosis factor ligand superfamily 3D structures]] | ||
| + | *[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Almo SC]] | ||
| + | [[Category: Chattopadhyay K]] | ||
| + | [[Category: Nathenson SG]] | ||
| + | [[Category: Ramagopal UA]] | ||
Current revision
Crystal Structure of mouse GITRL at 2.5 A.
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