1jek

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jek]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JEK FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jek]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JEK FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1jek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jek RCSB], [http://www.ebi.ac.uk/pdbsum/1jek PDBsum]</span></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=1jek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jek RCSB], [http://www.ebi.ac.uk/pdbsum/1jek PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ENV_VILVK ENV_VILVK]] 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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Kim, P S.]]
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[[Category: Kim, P S]]
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[[Category: Malashkevich, V N.]]
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[[Category: Malashkevich, V N]]
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[[Category: Singh, M.]]
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[[Category: Singh, M]]
[[Category: Envelope glycoprotein]]
[[Category: Envelope glycoprotein]]
[[Category: Gp41]]
[[Category: Gp41]]

Revision as of 13:29, 25 December 2014

Visna TM CORE STRUCTURE

1jek, resolution 1.50Å

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