6a05: Difference between revisions

No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='6a05' size='340' side='right'caption='[[6a05]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6a05' size='340' side='right'caption='[[6a05]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6a05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A05 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6a05]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A05 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1YD:2-amino-9-[(2R,3R,3aR,5S,7aS,9R,10R,10aR,12R,14aS)-9-(6-amino-9H-purin-9-yl)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecin-2-yl]-1,9-dihydro-6H-purin-6-one'>1YD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TMEM173, STING ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1YD:2-amino-9-[(2R,3R,3aR,5S,7aS,9R,10R,10aR,12R,14aS)-9-(6-amino-9H-purin-9-yl)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecin-2-yl]-1,9-dihydro-6H-purin-6-one'>1YD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6a05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a05 OCA], [http://pdbe.org/6a05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a05 RCSB], [http://www.ebi.ac.uk/pdbsum/6a05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a05 ProSAT]</span></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=6a05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a05 OCA], [https://pdbe.org/6a05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a05 RCSB], [https://www.ebi.ac.uk/pdbsum/6a05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a05 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/STING_PIG STING_PIG]
The cyclic dinucleotide (CDN)-stimulator of interferon genes (STING) pathway plays an important role in the detection of viral and bacterial pathogens in animals. Previous studies have shown that the metazoan second messenger cyclic GMP (2',5')-AMP (3',5') (2',3' cGAMP) generated by cyclic GAM-AMP synthase (cGAS) binds STING with high affinity compared with bacterial CDNs such as c-di-GMP, c-diAMP, and 3',3' cGAMP. Despite recent progress indicating that the CDN-binding domain (CBD) of dimeric STING binds asymmetric 2',3' cGAMP preferentially over symmetric 3',3' CDNs, it remains an open question whether STING molecules, such as human STING, adopt a symmetric dimeric conformation to efficiently engage its asymmetric ligand. Here, structural studies of the CBD from porcine STING (STING(CBD)) in complex with CDNs at 1.76-2.6 A resolutions revealed that porcine STING(CBD), unlike its human and mouse counterparts, can adopt an asymmetric ligand-binding pocket to accommodate the CDNs. We observed that the extensive interactions and shape complementarity between asymmetric 2',3' cGAMP and the ligand-binding pocket make it the most preferred ligand for porcine STING and that geometry constraints limit the binding between symmetric 3',3' CDN and porcine STING. The ligand-discrimination mechanism of porcine STING observed here expands our understanding of how the CDN-STING pathway is activated and of its role in antiviral defense.


Crystal structures of porcine STING(CBD)-CDN complexes reveal the mechanism of ligand recognition and discrimination of STING proteins.,Cong X, Yuan Z, Du Y, Wu B, Lu D, Wu X, Zhang Y, Li F, Wei B, Li J, Wu J, Xu S, Wang J, Qi J, Shang G, Gu L J Biol Chem. 2019 Jun 5. pii: RA119.007367. doi: 10.1074/jbc.RA119.007367. PMID:31167783<ref>PMID:31167783</ref>
==See Also==
 
*[[Stimulator of interferon genes protein|Stimulator of interferon genes protein]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
*[[Stimulator of interferon genes protein 3D structures|Stimulator of interferon genes protein 3D structures]]
</div>
<div class="pdbe-citations 6a05" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pig]]
[[Category: Sus scrofa]]
[[Category: Cong, X Y]]
[[Category: Cong XY]]
[[Category: Gu, L C]]
[[Category: Gu LC]]
[[Category: Shang, G J]]
[[Category: Shang GJ]]
[[Category: Yuan, Z L]]
[[Category: Yuan ZL]]
[[Category: Psting]]
[[Category: Signaling protein]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA