1y4m

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{{STRUCTURE_1y4m| PDB=1y4m | SCENE= }}
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==Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)==
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===Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)===
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<StructureSection load='1y4m' size='340' side='right' caption='[[1y4m]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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{{ABSTRACT_PUBMED_16140326}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1y4m]] is a 3 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=1Y4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y4M FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mof|1mof]], [[1mg1|1mg1]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERVFRDE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y4m RCSB], [http://www.ebi.ac.uk/pdbsum/1y4m PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y4/1y4m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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HERV-FRD is a human endogenous retrovirus that entered the human genome 40 million years ago. Its envelope gene, syncytin-2, was diverted by an ancestral host most probably because of its fusogenic property, for a role in placenta morphogenesis. It was maintained in a functional state in all primate branches as a bona fide cellular gene, submitted to a very low mutation rate as compared to infectious retrovirus genomes. The structure of the syncytin-2 protein thus provides a good insight into that of the oldest mammalian retroviral envelope. Here, we report the crystal structure of a central fragment of its "fossil" ectodomain, allowing a remarkable superposition with the structures of the corresponding domains of present-day infectious retroviruses, in spite of a more than 60% divergent sequence. These results suggest the existence of a unique structural solution selected by these proteins for their fusogenic function.
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==Function==
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Crystal structure of a pivotal domain of human syncytin-2, a 40 million years old endogenous retrovirus fusogenic envelope gene captured by primates.,Renard M, Varela PF, Letzelter C, Duquerroy S, Rey FA, Heidmann T J Mol Biol. 2005 Oct 7;352(5):1029-34. PMID:16140326<ref>PMID:16140326</ref>
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[[http://www.uniprot.org/uniprot/EFR1_HUMAN EFR1_HUMAN]] Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has retained its original fusogenic properties. Can make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity.<ref>PMID:14557543</ref> <ref>PMID:14694139</ref> SU mediates receptor recognition (By similarity).<ref>PMID:14557543</ref> <ref>PMID:14694139</ref> TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity).<ref>PMID:14557543</ref> <ref>PMID:14694139</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[1y4m]] is a 3 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=1Y4M OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:016140326</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Duquerroy, S.]]
[[Category: Duquerroy, S.]]

Revision as of 08:20, 3 October 2014

Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)

1y4m, resolution 1.60Å

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