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| | <StructureSection load='3g21' size='340' side='right'caption='[[3g21]], [[Resolution|resolution]] 0.90Å' scene=''> | | <StructureSection load='3g21' size='340' side='right'caption='[[3g21]], [[Resolution|resolution]] 0.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g21]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rsv-prc Rsv-prc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G21 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g21]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rous_sarcoma_virus_-_Prague_C Rous sarcoma virus - Prague C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G21 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 0.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3g0v|3g0v]], [[3g1g|3g1g]], [[3g1i|3g1i]], [[3g26|3g26]], [[3g28|3g28]], [[3g29|3g29]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11888 RSV-PrC])</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=3g21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g21 OCA], [https://pdbe.org/3g21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g21 RCSB], [https://www.ebi.ac.uk/pdbsum/3g21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g21 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=3g21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g21 OCA], [https://pdbe.org/3g21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g21 RCSB], [https://www.ebi.ac.uk/pdbsum/3g21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g21 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GAG_RSVP GAG_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/GAG_RSVP GAG_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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rsv-prc]] | + | [[Category: Rous sarcoma virus - Prague C]] |
| - | [[Category: Kingston, R L]] | + | [[Category: Kingston RL]] |
| - | [[Category: Alpha-helical bundle]]
| + | |
| - | [[Category: Capsid protein]]
| + | |
| - | [[Category: Retrovirus]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Virion]]
| + | |
| Structural highlights
Function
GAG_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).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In mature retroviral particles, the capsid protein (CA) forms a shell encasing the viral replication complex. Human immunodeficiency virus (HIV) CA dimerizes in solution, through its C-terminal domain (CTD), and this interaction is important for capsid assembly. In contrast, other retroviral capsid proteins, including that of Rous sarcoma virus (RSV), do not dimerize with measurable affinity. Here we show, using X-ray crystallography and other biophysical methods, that acidification causes RSV CA to dimerize in a fashion analogous to HIV CA, and that this drives capsid assembly in vitro. A pair of aspartic acid residues, located within the CTD dimer interface, explains why dimerization is linked to proton binding. Our results show that despite overarching structural similarities, the intermolecular forces responsible for forming and stabilizing the retroviral capsid differ markedly across retroviral genera. Our data further suggest that proton binding may regulate RSV capsid assembly, or modulate stability of the assembled capsid.
Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly.,Bailey GD, Hyun JK, Mitra AK, Kingston RL Structure. 2009 May 13;17(5):737-48. PMID:19446529[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bailey GD, Hyun JK, Mitra AK, Kingston RL. Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly. Structure. 2009 May 13;17(5):737-48. PMID:19446529 doi:10.1016/j.str.2009.03.010
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