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000018855 0247_ $$2DOI$$a10.1016/j.immuni.2011.07.012
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000018855 084__ $$2WoS$$aImmunology
000018855 1001_ $$0P:(DE-HGF)0$$aGao, S$$b0
000018855 245__ $$aStructure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function
000018855 260__ $$a[Cambridge, Mass.]$$bCell Press$$c2011
000018855 300__ $$a514 - 525
000018855 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000018855 440_0 $$023743$$aImmunity$$v35$$x1074-7613$$y4
000018855 500__ $$3POF3_Assignment on 2016-02-29
000018855 500__ $$aThis project was supported by grants of the Deutsche Forschungsgemeinschaft (SFB 740/TP C7 and SFB958/A12 to O.D. and Ko1579/8-1 to G.K.), by a Career Development Fellowship of The International Human Frontier Science Program Organization, and by the EMBO Young Investigator Program to O.D. We are grateful to A. Brunger for providing us with the prerelease of CNS version 1.3, the BESSY staff at beamline BL14.1 and SLS staff at beamline X06SA for help with data collection, and S. Werner, S. Paeschke, and S. Gruber for technical assistance.
000018855 520__ $$aHuman myxovirus resistance protein 1 (MxA) is an interferon-induced dynamin-like GTPase that acts as a cell-autonomous host restriction factor against many viral pathogens including influenza viruses. To study the molecular principles of its antiviral activity, we determined the crystal structure of nucleotide-free MxA, which showed an extended three-domain architecture. The central bundle signaling element (BSE) connected the amino-terminal GTPase domain with the stalk via two hinge regions. MxA oligomerized in the crystal via the stalk and the BSE, which in turn interacted with the stalk of the neighboring monomer. We demonstrated that the intra- and intermolecular domain interplay between the BSE and stalk was essential for oligomerization and the antiviral function of MxA. Based on these results, we propose a structural model for the mechano-chemical coupling in ring-like MxA oligomers as the principle mechanism for this unique antiviral effector protein.
000018855 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000018855 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000018855 588__ $$aDataset connected to Web of Science, Pubmed
000018855 650_2 $$2MeSH$$aAnimals
000018855 650_2 $$2MeSH$$aCell Line
000018855 650_2 $$2MeSH$$aCrystallography, X-Ray
000018855 650_2 $$2MeSH$$aGTP-Binding Proteins: chemistry
000018855 650_2 $$2MeSH$$aHumans
000018855 650_2 $$2MeSH$$aModels, Molecular
000018855 650_2 $$2MeSH$$aProtein Structure, Quaternary
000018855 650_2 $$2MeSH$$aProtein Structure, Tertiary
000018855 650_2 $$2MeSH$$aStructural Homology, Protein
000018855 650_7 $$00$$2NLM Chemicals$$amyxovirus resistance proteins
000018855 650_7 $$0EC 3.6.1.-$$2NLM Chemicals$$aGTP-Binding Proteins
000018855 650_7 $$2WoSType$$aJ
000018855 7001_ $$0P:(DE-HGF)0$$avon der Malsburg, A.$$b1
000018855 7001_ $$0P:(DE-HGF)0$$aDick, A.$$b2
000018855 7001_ $$0P:(DE-HGF)0$$aFaelber, K.$$b3
000018855 7001_ $$0P:(DE-Juel1)132018$$aSchröder, G.F.$$b4$$uFZJ
000018855 7001_ $$0P:(DE-HGF)0$$aHaller, O.$$b5
000018855 7001_ $$0P:(DE-HGF)0$$aKochs, G.$$b6
000018855 7001_ $$0P:(DE-HGF)0$$aDaumke, O.$$b7
000018855 773__ $$0PERI:(DE-600)2001966-X$$a10.1016/j.immuni.2011.07.012$$gVol. 35, p. 514 - 525$$p514 - 525$$q35<514 - 525$$tImmunity$$v35$$x1074-7613$$y2011
000018855 8567_ $$uhttp://dx.doi.org/10.1016/j.immuni.2011.07.012
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