5ha6

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m (Protected "5ha6" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5ha6 is ON HOLD until Paper Publication
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==Crystal structure of human syncytin-1 fusion subunit==
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<StructureSection load='5ha6' size='340' side='right' caption='[[5ha6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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Authors: Aydin, H., Lee, J.E.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ha6]] is a 2 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=5HA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HA6 FirstGlance]. <br>
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Description: Crystal structure of the human glycoprotein S
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERVW-1, ERVWE1 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ha6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ha6 OCA], [http://pdbe.org/5ha6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ha6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ha6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ha6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SYCY1_HUMAN SYCY1_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. May induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449, PubMed:12050356, PubMed:23492904).<ref>PMID:10708449</ref> <ref>PMID:12050356</ref> <ref>PMID:23492904</ref> Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of membranes.
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Human]]
[[Category: Aydin, H]]
[[Category: Aydin, H]]
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[[Category: Lee, J.E]]
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[[Category: Lee, J E]]
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[[Category: Cell adhesion]]
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[[Category: Fusion]]
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[[Category: Glycoprotein]]

Revision as of 09:15, 1 November 2017

Crystal structure of human syncytin-1 fusion subunit

5ha6, resolution 2.00Å

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