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| | ==NMR structure of the Rous sarcoma virus matrix protein (M-domain) in the presence of myo-inositol hexakisphosphate== | | ==NMR structure of the Rous sarcoma virus matrix protein (M-domain) in the presence of myo-inositol hexakisphosphate== |
| - | <StructureSection load='6ce5' size='340' side='right' caption='[[6ce5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6ce5' size='340' side='right'caption='[[6ce5]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ce5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rsv-prc Rsv-prc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CE5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ce5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rous_sarcoma_virus_-_Prague_C Rous sarcoma virus - Prague C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CE5 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ccj|6ccj]]</td></tr> | + | </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=6ce5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ce5 OCA], [https://pdbe.org/6ce5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ce5 RCSB], [https://www.ebi.ac.uk/pdbsum/6ce5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ce5 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11888 RSV-PrC])</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=6ce5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ce5 OCA], [http://pdbe.org/6ce5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ce5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ce5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ce5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/POL_RSVP POL_RSVP]] Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (By similarity). | + | [https://www.uniprot.org/uniprot/POL_RSVP POL_RSVP] Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6ce5" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ce5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rsv-prc]] | + | [[Category: Large Structures]] |
| - | [[Category: Saad, J S]] | + | [[Category: Rous sarcoma virus - Prague C]] |
| - | [[Category: Vlach, J]] | + | [[Category: Saad JS]] |
| - | [[Category: Asv]] | + | [[Category: Vlach J]] |
| - | [[Category: Gag]]
| + | |
| - | [[Category: Ip6]]
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| - | [[Category: Rsv]]
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| - | [[Category: Viral protein]]
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| Structural highlights
Function
POL_RSVP Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (By similarity).
Publication Abstract from PubMed
For most retroviruses, including HIV-1, binding of the Gag polyprotein to the plasma membrane (PM) is mediated by interactions between Gag's N-terminal myristoylated matrix (MA) domain and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) in the PM. The Gag protein of avian sarcoma virus (ASV) lacks the N-myristoylation signal but contains structural domains having functions similar to those of HIV-1 Gag. The molecular mechanism by which ASV Gag binds to the PM is incompletely understood. Here, we employed NMR techniques to elucidate the molecular determinants of the membrane-binding domain of ASV MA (MA87) to lipids and liposomes. We report that MA87 binds to the polar head of phosphoinositides such as PI(4,5)P2. We found that MA87 binding to inositol phosphates (IPs) is significantly enhanced by increasing the number of phosphate groups, indicating that the MA87-IP binding is governed by charge-charge interactions. Using a sensitive NMR-based liposome-binding assay, we show that binding of MA87 to liposomes is enhanced by incorporation of PI(4,5)P2 and phosphatidylserine. We also show that membrane binding is mediated by a basic surface formed by Lys-6, Lys-13, Lys-23, and Lys-24. Substitution of these residues to glutamate abolished binding of MA87 to both IPs and liposomes. In a joint manuscript, we further report that mutation of these lysine residues diminishes Gag assembly on the PM and inhibits ASV particle release. These findings provide a molecular basis for ASV Gag binding to the inner leaflet of the PM and advance our understanding of the basic mechanisms of retroviral assembly.
Structural basis for targeting avian sarcoma virus Gag polyprotein to the plasma membrane for virus assembly.,Vlach J, Eastep GN, Ghanam RH, Watanabe SM, Carter C, Saad JS J Biol Chem. 2018 Oct 11. pii: RA118.003944. doi: 10.1074/jbc.RA118.003944. PMID:30309983[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vlach J, Eastep GN, Ghanam RH, Watanabe SM, Carter C, Saad JS. Structural basis for targeting avian sarcoma virus Gag polyprotein to the plasma membrane for virus assembly. J Biol Chem. 2018 Oct 11. pii: RA118.003944. doi: 10.1074/jbc.RA118.003944. PMID:30309983 doi:http://dx.doi.org/10.1074/jbc.RA118.003944
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