2h95: Difference between revisions

<StructureSection load='2h95' size='340' side='right'caption='[[2h95]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2h95]] is a 4 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H95 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h95 OCA], [https://pdbe.org/2h95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h95 RCSB], [https://www.ebi.ac.uk/pdbsum/2h95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h95 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/M2_I77AB M2_I77AB]] Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation (By similarity).

[[Category: Asbury, T]]

[[Category: Cross, T A]]

[[Category: Hu, J]]

[[Category: Protein-ligand]]