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| | ==Atomic-Resolution Structure of HIV-1 Capsid Tubes by Magic Angle Spinning NMR== | | ==Atomic-Resolution Structure of HIV-1 Capsid Tubes by Magic Angle Spinning NMR== |
| - | <StructureSection load='6x63' size='340' side='right'caption='[[6x63]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='6x63' size='340' side='right'caption='[[6x63]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6x63]] is a 378 chain structure with sequence from [https://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X63 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6x63]] is a 378 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X63 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6wap|6wap]]</div></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=6x63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x63 OCA], [https://pdbe.org/6x63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x63 RCSB], [https://www.ebi.ac.uk/pdbsum/6x63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x63 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Gag-pol ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])</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=6x63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x63 OCA], [https://pdbe.org/6x63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x63 RCSB], [https://www.ebi.ac.uk/pdbsum/6x63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x63 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GAG_HV1N5 GAG_HV1N5]] Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu. Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity).
| + | [https://www.uniprot.org/uniprot/GAG_HV1N5 GAG_HV1N5] Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu. Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity). |
| | <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: Human immunodeficiency virus 1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bryer, A]] | + | [[Category: Bryer A]] |
| - | [[Category: Gronenborn, A M]] | + | [[Category: Gronenborn AM]] |
| - | [[Category: Hou, G]] | + | [[Category: Hou G]] |
| - | [[Category: Lu, M]] | + | [[Category: Lu M]] |
| - | [[Category: Perilla, J R]] | + | [[Category: Perilla JR]] |
| - | [[Category: Polenova, T]] | + | [[Category: Polenova T]] |
| - | [[Category: Quinn, C M]] | + | [[Category: Quinn CM]] |
| - | [[Category: Russell, R W]] | + | [[Category: Russell RW]] |
| - | [[Category: Schwieters, C D]] | + | [[Category: Schwieters CD]] |
| - | [[Category: Zhang, H]] | + | [[Category: Zhang H]] |
| - | [[Category: Ca protein assembly]]
| + | |
| - | [[Category: Hiv-1 capsid]]
| + | |
| - | [[Category: Hiv-aid]]
| + | |
| - | [[Category: Magic angle spinning nmr]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
GAG_HV1N5 Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu. Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity).
Publication Abstract from PubMed
HIV-1 capsid plays multiple key roles in viral replication, and inhibition of capsid assembly is an attractive target for therapeutic intervention. Here, we report the atomic-resolution structure of capsid protein (CA) tubes, determined by magic-angle spinning NMR and data-guided molecular dynamics simulations. Functionally important regions, including the NTD beta-hairpin, the cyclophilin A-binding loop, residues in the hexamer central pore, and the NTD-CTD linker region, are well defined. The structure of individual CA chains, their arrangement in the pseudo-hexameric units of the tube and the inter-hexamer interfaces are consistent with those in intact capsids and substantially different from the organization in crystal structures, which feature flat hexamers. The inherent curvature in the CA tubes is controlled by conformational variability of residues in the linker region and of dimer and trimer interfaces. The present structure reveals atomic-level detail in capsid architecture and provides important guidance for the design of novel capsid inhibitors.
Atomic-resolution structure of HIV-1 capsid tubes by magic-angle spinning NMR.,Lu M, Russell RW, Bryer AJ, Quinn CM, Hou G, Zhang H, Schwieters CD, Perilla JR, Gronenborn AM, Polenova T Nat Struct Mol Biol. 2020 Sep;27(9):863-869. doi: 10.1038/s41594-020-0489-2. Epub, 2020 Sep 8. PMID:32901160[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lu M, Russell RW, Bryer AJ, Quinn CM, Hou G, Zhang H, Schwieters CD, Perilla JR, Gronenborn AM, Polenova T. Atomic-resolution structure of HIV-1 capsid tubes by magic-angle spinning NMR. Nat Struct Mol Biol. 2020 Sep;27(9):863-869. doi: 10.1038/s41594-020-0489-2. Epub, 2020 Sep 8. PMID:32901160 doi:http://dx.doi.org/10.1038/s41594-020-0489-2
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