6ism: Difference between revisions

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 <StructureSection load='6ism' size='340' side='right'caption='[[6ism]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ism]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ISM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ISM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ism]] is a 1 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=6ISM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ISM FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ism FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ism OCA], [http://pdbe.org/6ism PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ism RCSB], [http://www.ebi.ac.uk/pdbsum/6ism PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ism ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</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=6ism FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ism OCA], [https://pdbe.org/6ism PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ism RCSB], [https://www.ebi.ac.uk/pdbsum/6ism PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ism ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BT3A1_HUMAN BT3A1_HUMAN]] Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate.<ref>PMID:21113407</ref> <ref>PMID:21918970</ref> <ref>PMID:22767497</ref> <ref>PMID:22846996</ref>
+[https://www.uniprot.org/uniprot/BT3A1_HUMAN BT3A1_HUMAN] Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate.<ref>PMID:21113407</ref> <ref>PMID:21918970</ref> <ref>PMID:22767497</ref> <ref>PMID:22846996</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Human Vgamma9Vdelta2 T cells respond to microbial infections and malignancy by sensing diphosphate-containing metabolites called phosphoantigens, which bind to the intracellular domain of butyrophilin 3A1, triggering extracellular interactions with the Vgamma9Vdelta2 T cell receptor (TCR). Here, we examined the molecular basis of this "inside-out" triggering mechanism. Crystal structures of intracellular butyrophilin 3A proteins alone or in complex with the potent microbial phosphoantigen HMBPP or a synthetic analog revealed key features of phosphoantigens and butyrophilins required for gammadelta T cell activation. Analyses with chemical probes and molecular dynamic simulations demonstrated that dimerized intracellular proteins cooperate in sensing HMBPP to enhance the efficiency of gammadelta T cell activation. HMBPP binding to butyrophilin doubled the binding force between a gammadelta T cell and a target cell during "outside" signaling, as measured by single-cell force microscopy. Our findings provide insight into the "inside-out" triggering of Vgamma9Vdelta2 T cell activation by phosphoantigen-bound butyrophilin, facilitating immunotherapeutic drug design.
+A Structural Change in Butyrophilin upon Phosphoantigen Binding Underlies Phosphoantigen-Mediated Vgamma9Vdelta2 T Cell Activation.,Yang Y, Li L, Yuan L, Zhou X, Duan J, Xiao H, Cai N, Han S, Ma X, Liu W, Chen CC, Wang L, Li X, Chen J, Kang N, Chen J, Shen Z, Malwal SR, Liu W, Shi Y, Oldfield E, Guo RT, Zhang Y Immunity. 2019 Mar 14. pii: S1074-7613(19)30083-4. doi:, 10.1016/j.immuni.2019.02.016. PMID:30902636<ref>PMID:30902636</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6ism" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Cai, N N]]
+[[Category: Cai NN]]
-[[Category: Chen, C C]]
+[[Category: Chen CC]]
-[[Category: Guo, R T]]
+[[Category: Guo RT]]
-[[Category: Liu, W D]]
+[[Category: Liu WD]]
-[[Category: Yang, Y Y]]
+[[Category: Yang YY]]
-[[Category: Zhang, Y H]]
+[[Category: Zhang YH]]
-[[Category: Butyrophilin]]
-[[Category: Signaling protein]]