3c9j: Difference between revisions
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== | ==The Crystal structure of Transmembrane domain of M2 protein and Amantadine complex== | ||
[[3c9j]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9J OCA]. | <StructureSection load='3c9j' size='340' side='right'caption='[[3c9j]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3c9j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Hong_Kong/156/97(H5N1)) Influenza A virus (A/Hong Kong/156/97(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C9J FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9j OCA], [https://pdbe.org/3c9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c9j RCSB], [https://www.ebi.ac.uk/pdbsum/3c9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c9j ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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. | |||
==See Also== | ==See Also== | ||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
*[[Ion channels|Ion channels]] | |||
*[[M2 protein|M2 protein]] | *[[M2 protein|M2 protein]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: | [[Category: Acharya R]] | ||
[[Category: | [[Category: Salom D]] | ||
[[Category: | [[Category: Stouffer AL]] | ||
[[Category: | |||
Latest revision as of 12:33, 21 February 2024
The Crystal structure of Transmembrane domain of M2 protein and Amantadine complexThe Crystal structure of Transmembrane domain of M2 protein and Amantadine complex
Structural highlights
FunctionM2_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. See Also |
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