6vv5: Difference between revisions

<table><tr><td colspan='2'>[[6vv5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pedv Pedv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VV5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VV5 FirstGlance]. <br>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vv5 OCA], [http://pdbe.org/6vv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vv5 RCSB], [http://www.ebi.ac.uk/pdbsum/6vv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vv5 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/S5RJN4_9ALPC S5RJN4_9ALPC]] S1 region attaches the virion to the cell membrane by interacting with host 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.[HAMAP-Rule:MF_04200]