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| | <StructureSection load='2ykd' size='340' side='right'caption='[[2ykd]], [[Resolution|resolution]] 1.86Å' scene=''> | | <StructureSection load='2ykd' size='340' side='right'caption='[[2ykd]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ykd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrsv Hrsv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ykd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_orthopneumovirus Human orthopneumovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vqp|2vqp]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
| - | <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=2ykd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykd OCA], [http://pdbe.org/2ykd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ykd RCSB], [http://www.ebi.ac.uk/pdbsum/2ykd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykd ProSAT]</span></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=2ykd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykd OCA], [https://pdbe.org/2ykd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ykd RCSB], [https://www.ebi.ac.uk/pdbsum/2ykd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MATRX_HRSVA MATRX_HRSVA]] Has a crucial role in virus assembly and budding. The matrix interacts with the RNP complex and this association serves two functions: facilitate virion assembly and inhibit the viral transcriptase activity. Early in infection, M is localized to the nucleus and may inhibit host cell transcription. Later on, M can associate with lipid rafts supposely by interacting with the cytoskeleton and with the cytoplasmic tail of glycoprotein G. The binding of M to host membrane is stabilized by the surface expression of the viral glycoproteins. These interactions may allow virus formation by mediating association of the nucleocapsid with the nascent envelop.<ref>PMID:11907323</ref> | + | [https://www.uniprot.org/uniprot/MATRX_HRSVA MATRX_HRSVA] Has a crucial role in virus assembly and budding. The matrix interacts with the RNP complex and this association serves two functions: facilitate virion assembly and inhibit the viral transcriptase activity. Early in infection, M is localized to the nucleus and may inhibit host cell transcription. Later on, M can associate with lipid rafts supposely by interacting with the cytoskeleton and with the cytoplasmic tail of glycoprotein G. The binding of M to host membrane is stabilized by the surface expression of the viral glycoproteins. These interactions may allow virus formation by mediating association of the nucleocapsid with the nascent envelop.<ref>PMID:11907323</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hrsv]] | + | [[Category: Human orthopneumovirus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beeby, A]] | + | [[Category: Beeby A]] |
| - | [[Category: Carlisle, J L]] | + | [[Category: Carlisle JL]] |
| - | [[Category: McPhee, H K]] | + | [[Category: McPhee HK]] |
| - | [[Category: Money, V A]] | + | [[Category: Money VA]] |
| - | [[Category: Sanderson, J M]] | + | [[Category: Sanderson JM]] |
| - | [[Category: Watson, S M.D]] | + | [[Category: Watson SMD]] |
| - | [[Category: Yeo, R P]] | + | [[Category: Yeo RP]] |
| - | [[Category: Peripheral membrane protein]]
| + | |
| - | [[Category: Viral matrix protein]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Virion]]
| + | |
| Structural highlights
Function
MATRX_HRSVA Has a crucial role in virus assembly and budding. The matrix interacts with the RNP complex and this association serves two functions: facilitate virion assembly and inhibit the viral transcriptase activity. Early in infection, M is localized to the nucleus and may inhibit host cell transcription. Later on, M can associate with lipid rafts supposely by interacting with the cytoskeleton and with the cytoplasmic tail of glycoprotein G. The binding of M to host membrane is stabilized by the surface expression of the viral glycoproteins. These interactions may allow virus formation by mediating association of the nucleocapsid with the nascent envelop.[1]
Publication Abstract from PubMed
The propensity of a matrix protein from an enveloped virus of the Mononegavirales family to associate with lipids representative of the viral envelope has been determined using label-free methods, including tensiometry and Brewster angle microscopy on lipid films at the air-water interface and atomic force microscopy on monolayers transferred to OTS-treated silicon wafers. This has enabled factors that influence the disposition of the protein with respect to the lipid interface to be characterized. In the absence of sphingomyelin, respiratory syncytial virus matrix protein penetrates monolayers composed of mixtures of phosphocholines with phosphoethanolamines or cholesterol at the air-water interface. In ternary mixtures composed of sphingomyelin, 1,2-dioleoyl-sn-glycero-3-phosphocholine, and cholesterol, the protein exhibits two separate behaviors: (1) peripheral association with the surface of sphingomyelin-rich domains and (2) penetration of sphingomyelin-poor domains. Prolonged incubation of the protein with mixtures of phosphocholines and phosphoethanolamines leads to the formation of helical protein assemblies of uniform diameter that demonstrate an inherent propensity of the protein to assemble into a filamentous form.
Influence of lipids on the interfacial disposition of respiratory syncytical virus matrix protein.,McPhee HK, Carlisle JL, Beeby A, Money VA, Watson SM, Yeo RP, Sanderson JM Langmuir. 2011 Jan 4;27(1):304-11. Epub 2010 Dec 9. PMID:21141948[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghildyal R, Mills J, Murray M, Vardaxis N, Meanger J. Respiratory syncytial virus matrix protein associates with nucleocapsids in infected cells. J Gen Virol. 2002 Apr;83(Pt 4):753-7. PMID:11907323
- ↑ McPhee HK, Carlisle JL, Beeby A, Money VA, Watson SM, Yeo RP, Sanderson JM. Influence of lipids on the interfacial disposition of respiratory syncytical virus matrix protein. Langmuir. 2011 Jan 4;27(1):304-11. Epub 2010 Dec 9. PMID:21141948 doi:10.1021/la104041n
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