5zxk
From Proteopedia
(Difference between revisions)
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<StructureSection load='5zxk' size='340' side='right'caption='[[5zxk]], [[Resolution|resolution]] 1.96Å' scene=''> | <StructureSection load='5zxk' size='340' side='right'caption='[[5zxk]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5zxk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZXK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zxk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZXK FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H6P:(2E)-4-HYDROXY-3-METHYLBUT-2-EN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>H6P</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BTN3A1, BTF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5zxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zxk OCA], [http://pdbe.org/5zxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zxk RCSB], [http://www.ebi.ac.uk/pdbsum/5zxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zxk ProSAT]</span></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=5zxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zxk OCA], [http://pdbe.org/5zxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zxk RCSB], [http://www.ebi.ac.uk/pdbsum/5zxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zxk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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> | [[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> | ||
| + | <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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5zxk" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chen, C C]] | [[Category: Chen, C C]] | ||
Revision as of 07:42, 10 April 2019
Crystal structure of intracellular B30.2 domain of BTN3A1 in complex with HMBPP
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Categories: Human | Large Structures | Chen, C C | Guo, R T | Liu, W D | Yang, Y Y | Zhang, Y H | Agonist | Signaling protein | Substrate binding
