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| | ==Crystal structure of the full-length Feline Immunodeficiency Virus capsid protein unveils original features== | | ==Crystal structure of the full-length Feline Immunodeficiency Virus capsid protein unveils original features== |
| - | <StructureSection load='5na2' size='340' side='right' caption='[[5na2]], [[Resolution|resolution]] 1.67Å' scene=''> | + | <StructureSection load='5na2' size='340' side='right'caption='[[5na2]], [[Resolution|resolution]] 1.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5na2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fiv Fiv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NA2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5na2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Feline_immunodeficiency_virus_(isolate_Petaluma) Feline immunodeficiency virus (isolate Petaluma)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NA2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.67Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11674 FIV])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5na2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5na2 OCA], [http://pdbe.org/5na2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5na2 RCSB], [http://www.ebi.ac.uk/pdbsum/5na2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5na2 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=5na2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5na2 OCA], [https://pdbe.org/5na2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5na2 RCSB], [https://www.ebi.ac.uk/pdbsum/5na2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5na2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GAG_FIVPE GAG_FIVPE]] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane (By similarity). Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p13 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). | + | [https://www.uniprot.org/uniprot/GAG_FIVPE GAG_FIVPE] Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane (By similarity). Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p13 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (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: Fiv]] | + | [[Category: Large Structures]] |
| - | [[Category: Alvarez, G]] | + | [[Category: Alvarez G]] |
| - | [[Category: Dujardin, M]] | + | [[Category: Dujardin M]] |
| - | [[Category: Folio, C]] | + | [[Category: Folio C]] |
| - | [[Category: Guillon, C]] | + | [[Category: Guillon C]] |
| - | [[Category: Sierra, N]] | + | [[Category: Sierra N]] |
| - | [[Category: Ca]]
| + | |
| - | [[Category: Capsid]]
| + | |
| - | [[Category: Feline immunodeficiency virus]]
| + | |
| - | [[Category: P24]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
GAG_FIVPE Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane (By similarity). Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p13 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).
Publication Abstract from PubMed
Feline immunodeficiency virus (FIV) is a member of the Retroviridae family. It is the causative agent of an acquired immunodeficiency syndrome (AIDS) in cats and wild felines. Its capsid protein (CA) drives the assembly of the viral particle, which is a critical step in the viral replication cycle. Here, the first atomic structure of full-length FIV CA to 1.67 A resolution is determined. The crystallized protein exhibits an original tetrameric assembly, composed of dimers which are stabilized by an intermolecular disulfide bridge induced by the crystallogenesis conditions. The FIV CA displays a standard alpha-helical CA topology with two domains, separated by a linker shorter than other retroviral CAs. The beta-hairpin motif at its amino terminal end, which interacts with nucleotides in HIV-1, is unusually long in FIV CA. Interestingly, this functional beta-motif is formed in this construct in the absence of the conserved N-terminal proline. The FIV CA exhibits a cis Arg-Pro bond in the CypA-binding loop, which is absent in known structures of lentiviral CAs. This structure represents the first tri-dimensional structure of a functional, full-length FIV CA.
Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal beta-Hairpin in the Absence of N-Terminal Proline.,Folio C, Sierra N, Dujardin M, Alvarez G, Guillon C Viruses. 2017 Nov 9;9(11). pii: v9110335. doi: 10.3390/v9110335. PMID:29120364[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Folio C, Sierra N, Dujardin M, Alvarez G, Guillon C. Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal beta-Hairpin in the Absence of N-Terminal Proline. Viruses. 2017 Nov 9;9(11). pii: v9110335. doi: 10.3390/v9110335. PMID:29120364 doi:http://dx.doi.org/10.3390/v9110335
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