32ul: Difference between revisions

Latest revision as of 09:15, 30 September 2026

Structure of ZNFX1 in the ATP-bound, pre-ATP hydrolysis state

Structural highlights

32ul is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.3Å
Ligands:	ATP, MG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ZNFX1_HUMAN The disease is caused by variants affecting the gene represented in this entry.

Function

ZNFX1_HUMAN RNA-binding protein that initiates the antiviral response and is required to restrict the replication of RNA viruses (PubMed:33872655). Acts as a double-stranded RNA (dsRNA) sensor that recognizes viral RNA and then interacts with MAVS to initiate the type I interferon response (By similarity). Also required for immunity against some bacteria, such as mycobacteria (PubMed:33876776).[UniProtKB:Q8R151]^[1] ^[2]

References

↑ Vavassori S, Chou J, Faletti LE, Haunerdinger V, Opitz L, Joset P, Fraser CJ, Prader S, Gao X, Schuch LA, Wagner M, Hoefele J, Maccari ME, Zhu Y, Elakis G, Gabbett MT, Forstner M, Omran H, Kaiser T, Kessler C, Olbrich H, Frosk P, Almutairi A, Platt CD, Elkins M, Weeks S, Rubin T, Planas R, Marchetti T, Koovely D, Klämbt V, Soliman NA, von Hardenberg S, Klemann C, Baumann U, Lenz D, Klein-Franke A, Schwemmle M, Huber M, Sturm E, Hartleif S, Häffner K, Gimpel C, Brotschi B, Laube G, Güngör T, Buckley MF, Kottke R, Staufner C, Hildebrandt F, Reu-Hofer S, Moll S, Weber A, Kaur H, Ehl S, Hiller S, Geha R, Roscioli T, Griese M, Pachlopnik Schmid J. Multisystem inflammation and susceptibility to viral infections in human ZNFX1 deficiency. J Allergy Clin Immunol. 2021 Aug;148(2):381-393. PMID:33872655 doi:10.1016/j.jaci.2021.03.045
↑ Le Voyer T, Neehus AL, Yang R, Ogishi M, Rosain J, Alroqi F, Alshalan M, Blumental S, Al Ali F, Khan T, Ata M, Rozen L, Demulder A, Bastard P, Gruber C, Roynard M, Seeleuthener Y, Rapaport F, Bigio B, Chrabieh M, Sng D, Berteloot L, Boddaert N, Rozenberg F, Al-Muhsen S, Bertoli-Avella A, Abel L, Bogunovic D, Marr N, Mansouri D, Al Mutairi F, Béziat V, Weil D, Mahdaviani SA, Ferster A, Zhang SY, Reversade B, Boisson-Dupuis S, Casanova JL, Bustamante J. Inherited deficiency of stress granule ZNFX1 in patients with monocytosis and mycobacterial disease. Proc Natl Acad Sci U S A. 2021 Apr 13;118(15):e2102804118. PMID:33876776 doi:10.1073/pnas.2102804118

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OCA

[1] Vavassori S, Chou J, Faletti LE, Haunerdinger V, Opitz L, Joset P, Fraser CJ, Prader S, Gao X, Schuch LA, Wagner M, Hoefele J, Maccari ME, Zhu Y, Elakis G, Gabbett MT, Forstner M, Omran H, Kaiser T, Kessler C, Olbrich H, Frosk P, Almutairi A, Platt CD, Elkins M, Weeks S, Rubin T, Planas R, Marchetti T, Koovely D, Klämbt V, Soliman NA, von Hardenberg S, Klemann C, Baumann U, Lenz D, Klein-Franke A, Schwemmle M, Huber M, Sturm E, Hartleif S, Häffner K, Gimpel C, Brotschi B, Laube G, Güngör T, Buckley MF, Kottke R, Staufner C, Hildebrandt F, Reu-Hofer S, Moll S, Weber A, Kaur H, Ehl S, Hiller S, Geha R, Roscioli T, Griese M, Pachlopnik Schmid J. Multisystem inflammation and susceptibility to viral infections in human ZNFX1 deficiency. J Allergy Clin Immunol. 2021 Aug;148(2):381-393. PMID:33872655 doi:10.1016/j.jaci.2021.03.045

[2] Le Voyer T, Neehus AL, Yang R, Ogishi M, Rosain J, Alroqi F, Alshalan M, Blumental S, Al Ali F, Khan T, Ata M, Rozen L, Demulder A, Bastard P, Gruber C, Roynard M, Seeleuthener Y, Rapaport F, Bigio B, Chrabieh M, Sng D, Berteloot L, Boddaert N, Rozenberg F, Al-Muhsen S, Bertoli-Avella A, Abel L, Bogunovic D, Marr N, Mansouri D, Al Mutairi F, Béziat V, Weil D, Mahdaviani SA, Ferster A, Zhang SY, Reversade B, Boisson-Dupuis S, Casanova JL, Bustamante J. Inherited deficiency of stress granule ZNFX1 in patients with monocytosis and mycobacterial disease. Proc Natl Acad Sci U S A. 2021 Apr 13;118(15):e2102804118. PMID:33876776 doi:10.1073/pnas.2102804118

[1]

[2]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 32ul is ON HOLD
+==Structure of ZNFX1 in the ATP-bound, pre-ATP hydrolysis state==
+<StructureSection load='32ul' size='340' side='right'caption='[[32ul]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[32ul]] 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=32UL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=32UL FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=32ul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=32ul OCA], [https://pdbe.org/32ul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=32ul RCSB], [https://www.ebi.ac.uk/pdbsum/32ul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=32ul ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ZNFX1_HUMAN ZNFX1_HUMAN] The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/ZNFX1_HUMAN ZNFX1_HUMAN] RNA-binding protein that initiates the antiviral response and is required to restrict the replication of RNA viruses (PubMed:33872655). Acts as a double-stranded RNA (dsRNA) sensor that recognizes viral RNA and then interacts with MAVS to initiate the type I interferon response (By similarity). Also required for immunity against some bacteria, such as mycobacteria (PubMed:33876776).[UniProtKB:Q8R151]<ref>PMID:33872655</ref> <ref>PMID:33876776</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Naydenova K]]
+[[Category: Randow F]]
+[[Category: Yip MCJ]]

32ul: Difference between revisions

Latest revision as of 09:15, 30 September 2026

Structure of ZNFX1 in the ATP-bound, pre-ATP hydrolysis state

Structural highlights

Disease

Function

References

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