4rwb
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Racemic influenza M2-TM crystallized from monoolein lipidic cubic phase== |
| - | + | <StructureSection load='4rwb' size='340' side='right' caption='[[4rwb]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4rwb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RWB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RWB FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPG:1-MONOOLEOYL-RAC-GLYCEROL'>MPG</scene></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> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rwc|4rwc]]</td></tr> | |
| - | [[Category: | + | <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=4rwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwb OCA], [http://pdbe.org/4rwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rwb RCSB], [http://www.ebi.ac.uk/pdbsum/4rwb PDBsum]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: Mortenson, D | + | == Function == |
| - | [[Category: | + | [[http://www.uniprot.org/uniprot/M2_I97A1 M2_I97A1]] 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. |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Forest, K T]] | ||
| + | [[Category: Gellman, S H]] | ||
| + | [[Category: Kreitler, D F]] | ||
| + | [[Category: Mortenson, D E]] | ||
| + | [[Category: Steinkruger, J D]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Proton channel]] | ||
| + | [[Category: Transmembrane peptide]] | ||
Revision as of 04:02, 16 October 2015
Racemic influenza M2-TM crystallized from monoolein lipidic cubic phase
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