2kqt

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<StructureSection load='2kqt' size='340' side='right'caption='[[2kqt]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''>
<StructureSection load='2kqt' size='340' side='right'caption='[[2kqt]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2kqt]] is a 4 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KQT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KQT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2kqt]] is a 4 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KQT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=308:(3S,5S,7S)-TRICYCLO[3.3.1.1~3,7~]DECAN-1-AMINE'>308</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=308:(3S,5S,7S)-TRICYCLO[3.3.1.1~3,7~]DECAN-1-AMINE'>308</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kad|2kad]], [[2h95|2h95]], [[2rlf|2rlf]], [[3c9j|3c9j]], [[1nyj|1nyj]], [[3bkd|3bkd]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2kad|2kad]], [[2h95|2h95]], [[2rlf|2rlf]], [[3c9j|3c9j]], [[1nyj|1nyj]], [[3bkd|3bkd]]</div></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=2kqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kqt OCA], [http://pdbe.org/2kqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kqt RCSB], [http://www.ebi.ac.uk/pdbsum/2kqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kqt ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kqt OCA], [https://pdbe.org/2kqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kqt RCSB], [https://www.ebi.ac.uk/pdbsum/2kqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kqt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q9YP62_9INFA Q9YP62_9INFA]] 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).[SAAS:SAAS002089_004_400258]
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[[https://www.uniprot.org/uniprot/Q9YP62_9INFA Q9YP62_9INFA]] 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).[SAAS:SAAS002089_004_400258]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Amantadine|Amantadine]]
 
*[[Ion channels 3D structures|Ion channels 3D structures]]
*[[Ion channels 3D structures|Ion channels 3D structures]]
*[[M2 protein|M2 protein]]
*[[M2 protein|M2 protein]]
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*[[Molecular Playground/Influenza A M2 transmembrane domain|Molecular Playground/Influenza A M2 transmembrane domain]]
 
== References ==
== References ==
<references/>
<references/>

Revision as of 07:09, 1 December 2021

Solid-state NMR structure of the M2 transmembrane peptide of the influenza A virus in DMPC lipid bilayers bound to deuterated amantadine

PDB ID 2kqt

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