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| Hauptseite > Publikationsdatenbank > Structure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function > print |
| Hauptseite > Publikationsdatenbank > Structure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function > print |
| 001 | 18855 | ||
| 005 | 20200402210136.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:21962493 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.immuni.2011.07.012 |
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| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 610 |
| 084 | _ | _ | |2 WoS |a Immunology |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Gao, S |b 0 |
| 245 | _ | _ | |a Structure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function |
| 260 | _ | _ | |a [Cambridge, Mass.] |b Cell Press |c 2011 |
| 300 | _ | _ | |a 514 - 525 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
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| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 23743 |a Immunity |v 35 |x 1074-7613 |y 4 |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-29 |
| 500 | _ | _ | |a This 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. |
| 520 | _ | _ | |a Human 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. |
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| 650 | _ | 2 | |2 MeSH |a GTP-Binding Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Quaternary |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Structural Homology, Protein |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a myxovirus resistance proteins |
| 650 | _ | 7 | |0 EC 3.6.1.- |2 NLM Chemicals |a GTP-Binding Proteins |
| 650 | _ | 7 | |2 WoSType |a J |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a von der Malsburg, A. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Dick, A. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Faelber, K. |b 3 |
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| 773 | _ | _ | |0 PERI:(DE-600)2001966-X |a 10.1016/j.immuni.2011.07.012 |g Vol. 35, p. 514 - 525 |p 514 - 525 |q 35<514 - 525 |t Immunity |v 35 |x 1074-7613 |y 2011 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1016/j.immuni.2011.07.012 |
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