3szr

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<StructureSection load='3szr' size='340' side='right'caption='[[3szr]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='3szr' size='340' side='right'caption='[[3szr]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3szr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3szr]] 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=3SZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZR FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ljb|3ljb]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MX1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3szr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3szr OCA], [https://pdbe.org/3szr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3szr RCSB], [https://www.ebi.ac.uk/pdbsum/3szr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3szr 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=3szr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3szr OCA], [https://pdbe.org/3szr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3szr RCSB], [https://www.ebi.ac.uk/pdbsum/3szr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3szr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MX1_HUMAN MX1_HUMAN]] Interferon-induced dynamin-like GTPase with antiviral activity against a wide range of RNA viruses and some DNA viruses. Its target viruses include negative-stranded RNA viruses and HBV through binding and inactivation of their ribonucleocapsid. May also antagonize reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV) replication by preventing the nuclear import of viral nucleocapsids. Inhibits La Crosse virus (LACV) replication by sequestering viral nucleoprotein in perinuclear complexes, preventing genome amplification, budding, and egress. Inhibits influenza A virus (IAV) replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Enhances ER stress-mediated cell death after influenza virus infection. May regulate the calcium channel activity of TRPCs.<ref>PMID:20603636</ref> <ref>PMID:11880649</ref> <ref>PMID:15047845</ref> <ref>PMID:14752052</ref> <ref>PMID:15355513</ref> <ref>PMID:14687945</ref> <ref>PMID:15757897</ref> <ref>PMID:16413306</ref> <ref>PMID:16202617</ref> <ref>PMID:17374778</ref> <ref>PMID:18668195</ref> <ref>PMID:19109387</ref> <ref>PMID:21900240</ref> <ref>PMID:21992152</ref>
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[https://www.uniprot.org/uniprot/MX1_HUMAN MX1_HUMAN] Interferon-induced dynamin-like GTPase with antiviral activity against a wide range of RNA viruses and some DNA viruses. Its target viruses include negative-stranded RNA viruses and HBV through binding and inactivation of their ribonucleocapsid. May also antagonize reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV) replication by preventing the nuclear import of viral nucleocapsids. Inhibits La Crosse virus (LACV) replication by sequestering viral nucleoprotein in perinuclear complexes, preventing genome amplification, budding, and egress. Inhibits influenza A virus (IAV) replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Enhances ER stress-mediated cell death after influenza virus infection. May regulate the calcium channel activity of TRPCs.<ref>PMID:20603636</ref> <ref>PMID:11880649</ref> <ref>PMID:15047845</ref> <ref>PMID:14752052</ref> <ref>PMID:15355513</ref> <ref>PMID:14687945</ref> <ref>PMID:15757897</ref> <ref>PMID:16413306</ref> <ref>PMID:16202617</ref> <ref>PMID:17374778</ref> <ref>PMID:18668195</ref> <ref>PMID:19109387</ref> <ref>PMID:21900240</ref> <ref>PMID:21992152</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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Structure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function.,Gao S, von der Malsburg A, Dick A, Faelber K, Schroder GF, Haller O, Kochs G, Daumke O Immunity. 2011 Sep 28. PMID:21962493<ref>PMID:21962493</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3szr" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Daumke, O]]
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[[Category: Daumke O]]
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[[Category: Gao, S]]
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[[Category: Gao S]]
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[[Category: Interferon-induced antiviral gtpase]]
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[[Category: Membrane associated]]
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[[Category: Protein binding]]
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Current revision

Crystal structure of modified nucleotide-free human MxA

PDB ID 3szr

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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