5yl9: Difference between revisions

<table><tr><td colspan='2'>[[5yl9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YL9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YL9 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yl9 OCA], [http://pdbe.org/5yl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yl9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yl9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yl9 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SPIKE_CVH22 SPIKE_CVH22]] S1 region attaches the virion to the cell membrane by interacting with human ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the 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) regions 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 (By similarity).  

[[Category: Meng, B]]

[[Category: WIlson, I A]]

[[Category: Yan, L]]

[[Category: Yang, B]]

[[Category: Viral protein]]