View source for 7lt1


==Structure of the cGAS-like receptor human MB21D2==
<StructureSection load='7lt1' size='340' side='right'caption='[[7lt1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LT1 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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'>[https://proteopedia.org/fgij/fg.htm?mol=7lt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lt1 OCA], [https://pdbe.org/7lt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lt1 RCSB], [https://www.ebi.ac.uk/pdbsum/7lt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lt1 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Cyclic GMP-AMP synthase (cGAS) is a cytosolic DNA sensor that produces the second messenger 2'3'-cGAMP and controls activation of innate immunity in mammalian cells(1-5). Animal genomes typically encode multiple proteins with predicted homology to cGAS(6-10), but the function of these uncharacterized enzymes is unknown. Here we show that cGAS-like receptors (cGLRs) are innate immune sensors capable of recognizing divergent molecular patterns and catalyzing synthesis of distinct nucleotide second messenger signals. Crystal structures of human and insect cGLRs reveal a nucleotidyltransferase signaling core shared with cGAS and a diversified primary ligand-binding surface modified with significant insertions and deletions. We demonstrate that cGLR surface remodeling enables altered ligand specificity and use a forward biochemical screen to identify cGLR1 as a double-stranded RNA sensor in the model organism Drosophila melanogaster. Surprisingly, RNA recognition activates Drosophila cGLR1 to synthesize the novel product cG[3'-5']pA[2'-5']p (3'2'-cGAMP). A crystal structure of Drosophila Stimulator of Interferon Genes (STING) in complex with 3'2'-cGAMP explains selective isomer recognition and we demonstrate that 3'2'-cGAMP induces an enhanced antiviral state in vivo that protects from viral infection. Similar to radiation of Toll-like receptors in pathogen immunity, our results establish cGLRs as a diverse family of metazoan pattern recognition receptors.

cGAS-like receptors sense RNA and control 3'2'-cGAMP signaling in Drosophila.,Slavik KM, Morehouse BR, Ragucci AE, Zhou W, Ai X, Chen Y, Li L, Wei Z, Bahre H, Konig M, Seifert R, Lee ASY, Cai H, Imler JL, Kranzusch PJ Nature. 2021 Jul 14. pii: 10.1038/s41586-021-03743-5. doi:, 10.1038/s41586-021-03743-5. PMID:34261127<ref>PMID:34261127</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Kranzusch PJ]]
[[Category: Morehouse BR]]
[[Category: Slavik KM]]