1y4m

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(Difference between revisions)

Revision as of 20:28, 9 September 2015

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

Structural highlights

1y4m is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1mof, 1mg1
Gene:	ERVFRDE1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[EFRD1_HUMAN] This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process (PubMed:18988732).^[1] Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139).^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Esnault C, Priet S, Ribet D, Vernochet C, Bruls T, Lavialle C, Weissenbach J, Heidmann T. A placenta-specific receptor for the fusogenic, endogenous retrovirus-derived, human syncytin-2. Proc Natl Acad Sci U S A. 2008 Nov 11;105(45):17532-7. doi:, 10.1073/pnas.0807413105. Epub 2008 Nov 6. PMID:18988732 doi:http://dx.doi.org/10.1073/pnas.0807413105
↑ Blaise S, Ruggieri A, Dewannieux M, Cosset FL, Heidmann T. Identification of an envelope protein from the FRD family of human endogenous retroviruses (HERV-FRD) conferring infectivity and functional conservation among simians. J Virol. 2004 Jan;78(2):1050-4. PMID:14694139
↑ Renard M, Varela PF, Letzelter C, Duquerroy S, Rey FA, Heidmann T. Crystal structure of a pivotal domain of human syncytin-2, a 40 million years old endogenous retrovirus fusogenic envelope gene captured by primates. J Mol Biol. 2005 Oct 7;352(5):1029-34. PMID:16140326 doi:10.1016/j.jmb.2005.07.058

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y4m"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mof|1mof]], [[1mg1|1mg1]]</td></tr>
 <tr id='gene'><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>
-<tr id='resources'><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>
+<tr id='resources'><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://pdbe.org/1y4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y4m RCSB], [http://www.ebi.ac.uk/pdbsum/1y4m PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[[http://www.uniprot.org/uniprot/EFRD1_HUMAN EFRD1_HUMAN]] This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process (PubMed:18988732).<ref>PMID:18988732</ref>   Endogenous envelope proteins may have kept, lost or modified their original function during evolution but this one can still make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein mediates receptor recognition, while the transmembrane protein 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 (PubMed:14694139).<ref>PMID:14694139</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1y4m" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1y4m

From Proteopedia

Revision as of 20:28, 9 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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