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5uot
From Proteopedia
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==CryoEM structure of the helical assembly of full length MxB== | ==CryoEM structure of the helical assembly of full length MxB== | ||
| - | < | + | <SX load='5uot' size='340' side='right' viewer='molstar' caption='[[5uot]], [[Resolution|resolution]] 4.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5uot]] is a 62 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UOT OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[5uot]] is a 62 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UOT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UOT FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5uot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uot OCA], [http://pdbe.org/5uot PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uot RCSB], [http://www.ebi.ac.uk/pdbsum/5uot PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uot ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | {{Large structure}} | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MX2_HUMAN MX2_HUMAN]] Interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1). Acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA. Exhibits antiviral activity also against simian immunodeficiency virus (SIV-mnd). May play a role in regulating nucleocytoplasmic transport and cell-cycle progression.<ref>PMID:15184662</ref> <ref>PMID:24048477</ref> <ref>PMID:24055605</ref> <ref>PMID:24121441</ref> | [[http://www.uniprot.org/uniprot/MX2_HUMAN MX2_HUMAN]] Interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1). Acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA. Exhibits antiviral activity also against simian immunodeficiency virus (SIV-mnd). May play a role in regulating nucleocytoplasmic transport and cell-cycle progression.<ref>PMID:15184662</ref> <ref>PMID:24048477</ref> <ref>PMID:24055605</ref> <ref>PMID:24121441</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human dynamin-like, interferon-induced myxovirus resistance 2 (Mx2 or MxB) is a potent HIV-1 inhibitor. Antiviral activity requires both the amino-terminal region of MxB and protein oligomerization, each of which has eluded structural determination due to difficulties in protein preparation. We report that maltose binding protein-fused, full-length wild-type MxB purifies as oligomers and further self-assembles into helical arrays in physiological salt. Guanosine triphosphate (GTP), but not guanosine diphosphate, binding results in array disassembly, whereas subsequent GTP hydrolysis allows its reformation. Using cryo-electron microscopy (cryoEM), we determined the MxB assembly structure at 4.6 A resolution, representing the first near-atomic resolution structure in the mammalian dynamin superfamily. The structure revealed previously described and novel MxB assembly interfaces. Mutational analyses demonstrated a critical role for one of the novel interfaces in HIV-1 restriction. | ||
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| + | CryoEM structure of MxB reveals a novel oligomerization interface critical for HIV restriction.,Alvarez FJD, He S, Perilla JR, Jang S, Schulten K, Engelman AN, Scheres SHW, Zhang P Sci Adv. 2017 Sep 15;3(9):e1701264. doi: 10.1126/sciadv.1701264. eCollection 2017, Sep. PMID:28929138<ref>PMID:28929138</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5uot" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Alvarez, F J.D]] | [[Category: Alvarez, F J.D]] | ||
[[Category: Perilla, J R]] | [[Category: Perilla, J R]] | ||
Current revision
CryoEM structure of the helical assembly of full length MxB
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Categories: Human | Large Structures | Alvarez, F J.D | Perilla, J R | Schulten, K | Zhang, P | Antiviral protein | Assembly | Cryoem | Dynamin | Helical reconstruction | Hiv-1 | Interferon | Molecular dynamic simulation | Mx2 | Mxb
