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| - | [[Image:1aa7.gif|left|200px]] | |
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| - | {{Structure
| + | ==INFLUENZA VIRUS MATRIX PROTEIN CRYSTAL STRUCTURE AT PH 4.0== |
| - | |PDB= 1aa7 |SIZE=350|CAPTION= <scene name='initialview01'>1aa7</scene>, resolution 2.08Å
| + | <StructureSection load='1aa7' size='340' side='right'caption='[[1aa7]], [[Resolution|resolution]] 2.08Å' scene=''> |
| - | |SITE= <scene name='pdbsite=S1:RNA-Binding+Site'>S1</scene>
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1aa7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AA7 FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08Å</td></tr> |
| - | |GENE=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa7 OCA], [https://pdbe.org/1aa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aa7 RCSB], [https://www.ebi.ac.uk/pdbsum/1aa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aa7 ProSAT]</span></td></tr> |
| - | |DOMAIN= | + | </table> |
| - | |RELATEDENTRY=
| + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa7 OCA], [http://www.ebi.ac.uk/pdbsum/1aa7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aa7 RCSB]</span> | + | [https://www.uniprot.org/uniprot/M1_I34A1 M1_I34A1] Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.<ref>PMID:11531417</ref> Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.<ref>PMID:11531417</ref> |
| - | }}
| + | == References == |
| - | | + | <references/> |
| - | '''INFLUENZA VIRUS MATRIX PROTEIN CRYSTAL STRUCTURE AT PH 4.0'''
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | | + | [[Category: Large Structures]] |
| - | ==Overview== | + | |
| - | Matrix protein (M1) of influenza virus is a bifunctional protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. It is therefore required that M1 binds both membrane and RNA simultaneously. The X-ray crystal structure of the N-terminal portion of type A influenza virus M1-amino acid residues 2-158-has been determined at 2.08 A resolution at pH 4.0. The protein forms a dimer. A highly positively charged region on the dimer surface is suitably positioned to bind RNA while the hydrophobic surface opposite the RNA binding region may be involved in interactions with the membrane. The membrane-binding hydrophobic surface could be buried or exposed after a conformational change.
| + | |
| - | | + | |
| - | ==About this Structure==
| + | |
| - | 1AA7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AA7 OCA].
| + | |
| - | | + | |
| - | ==Reference==
| + | |
| - | Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1., Sha B, Luo M, Nat Struct Biol. 1997 Mar;4(3):239-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9164466 9164466]
| + | |
| - | [[Category: Single protein]] | + | |
| | [[Category: Unidentified influenza virus]] | | [[Category: Unidentified influenza virus]] |
| - | [[Category: Luo, M.]] | + | [[Category: Luo M]] |
| - | [[Category: Sha, B.]] | + | [[Category: Sha B]] |
| - | [[Category: matrix protein]]
| + | |
| - | [[Category: transcription repressor]]
| + | |
| - | [[Category: viral assembly]]
| + | |
| - | [[Category: virion budding]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:36:30 2008''
| + | |
| Structural highlights
Function
M1_I34A1 Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.[1] Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.[2]
References
- ↑ Huang X, Liu T, Muller J, Levandowski RA, Ye Z. Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology. 2001 Sep 1;287(2):405-16. PMID:11531417 doi:10.1006/viro.2001.1067
- ↑ Huang X, Liu T, Muller J, Levandowski RA, Ye Z. Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology. 2001 Sep 1;287(2):405-16. PMID:11531417 doi:10.1006/viro.2001.1067
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