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<table><tr><td colspan='2'>[[2x8q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rsv-prc Rsv-prc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X8Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X8Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2x8q]] 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=2X8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X8Q FirstGlance]. <br>
[[http://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).
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[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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==See Also==
==See Also==
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*[[Virus coat protein|Virus coat protein]]
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Rsv-prc]]
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[[Category: Large Structures]]
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[[Category: Hyun, J K]]
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[[Category: Rous sarcoma virus - Prague C]]
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[[Category: Kingston, R L]]
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[[Category: K Hyun J]]
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[[Category: Mitra, A K]]
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[[Category: Kingston RL]]
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[[Category: Radjainia, M]]
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[[Category: Mitra AK]]
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[[Category: Capsid protein]]
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[[Category: Radjainia M]]
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[[Category: Viral matrix protein]]
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[[Category: Virus]]
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Current revision
Cryo-EM 3D model of the icosahedral particle composed of Rous sarcoma virus capsid protein pentamers
2x8q is a 1 chain structure with sequence from Rous sarcoma virus - Prague C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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
Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In a mature and infectious retroviral particle, the capsid protein (CA) forms a shell surrounding the genomic RNA and the replicative machinery of the virus. The irregular nature of this capsid shell precludes direct atomic resolution structural analysis. CA hexamers and pentamers are the fundamental building blocks of the capsid, however the pentameric state, in particular, remains poorly characterized. We have developed an efficient in vitro protocol for studying the assembly of Rous sarcoma virus (RSV) CA that involves mild acidification and produces structures modeling the authentic viral capsid. These structures include regular spherical particles with T = 1 icosahedral symmetry, built from CA pentamers alone. These particles were subject to cryoelectron microscopy (cryo-EM) and image processing, and a pseudo-atomic model of the icosahedron was created by docking atomic structures of the constituent CA domains into the cryo-EM-derived three-dimensional density map. The N-terminal domain (NTD) of CA forms pentameric turrets, which decorate the surface of the icosahedron, while the C-terminal domain (CTD) of CA is positioned underneath, linking the pentamers. Biophysical analysis of the icosahedral particle preparation reveals that CA monomers and icosahedra are the only detectable species and that these exist in reversible equilibrium at pH 5. These same acidic conditions are known to promote formation of a RSV CA CTD dimer, present within the icosahedral particle, which facilitates capsid assembly. The results are consistent with a model in which RSV CA assembly is a nucleation-limited process driven by very weak protein-protein interactions.
Proton-driven assembly of the Rous Sarcoma virus capsid protein results in the formation of icosahedral particles.,Hyun JK, Radjainia M, Kingston RL, Mitra AK J Biol Chem. 2010 May 14;285(20):15056-64. Epub 2010 Mar 12. PMID:20228062[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Hyun JK, Radjainia M, Kingston RL, Mitra AK. Proton-driven assembly of the Rous Sarcoma virus capsid protein results in the formation of icosahedral particles. J Biol Chem. 2010 May 14;285(20):15056-64. Epub 2010 Mar 12. PMID:20228062 doi:10.1074/jbc.M110.108209
