1y4m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:56, 6 November 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_1y4m| PDB=1y4m | SCENE= }}
 
-
===Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)===
 
-
{{ABSTRACT_PUBMED_16140326}}
 
-
==Function==
+
==Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)==
-
[[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>
+
<StructureSection load='1y4m' size='340' side='right'caption='[[1y4m]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1y4m]] is a 3 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=1Y4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y4M FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=1y4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4m OCA], [https://pdbe.org/1y4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y4m RCSB], [https://www.ebi.ac.uk/pdbsum/1y4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y4m ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SYCY2_HUMAN SYCY2_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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y4/1y4m_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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/main_output.php?pdb_ID=1y4m ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
==About this Structure==
+
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>
-
[[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].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:016140326</ref><references group="xtra"/><references/>
+
</div>
-
[[Category: Human]]
+
<div class="pdbe-citations 1y4m" style="background-color:#fffaf0;"></div>
-
[[Category: Duquerroy, S.]]
+
 
-
[[Category: Heidmann, T.]]
+
==See Also==
-
[[Category: Letzelter, C.]]
+
*[[Syncytin|Syncytin]]
-
[[Category: Renard, M.]]
+
== References ==
-
[[Category: Rey, F A.]]
+
<references/>
-
[[Category: Varela, P F.]]
+
__TOC__
-
[[Category: Coat protein]]
+
</StructureSection>
-
[[Category: Endogenous retrovirus]]
+
[[Category: Homo sapiens]]
-
[[Category: Membrane fusion]]
+
[[Category: Large Structures]]
-
[[Category: Membrane protein]]
+
[[Category: Duquerroy S]]
 +
[[Category: Heidmann T]]
 +
[[Category: Letzelter C]]
 +
[[Category: Renard M]]
 +
[[Category: Rey FA]]
 +
[[Category: Varela PF]]

Current revision

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

PDB ID 1y4m

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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