5h9c: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h9c OCA], [https://pdbe.org/5h9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h9c RCSB], [https://www.ebi.ac.uk/pdbsum/5h9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h9c ProSAT]</span></td></tr>

</table>

~~== Function ==~~

[https://www.uniprot.org/uniprot/ENV_RSVSA ENV_RSVSA] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has 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 viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).

== Publication Abstract from PubMed ==

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 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h9c OCA], [https://pdbe.org/5h9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h9c RCSB], [https://www.ebi.ac.uk/pdbsum/5h9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h9c ProSAT]</span></td></tr>
 </table>
-== Function ==
-[https://www.uniprot.org/uniprot/ENV_RSVSA ENV_RSVSA] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).  The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has 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 viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==