1eoq

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[[Image:1eoq.jpg|left|200px]]
 
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==ROUS SARCOMA VIRUS CAPSID PROTEIN: C-TERMINAL DOMAIN==
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The line below this paragraph, containing "STRUCTURE_1eoq", creates the "Structure Box" on the page.
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<StructureSection load='1eoq' size='340' side='right'caption='[[1eoq]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1eoq]] 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=1EOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eoq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eoq OCA], [https://pdbe.org/1eoq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eoq RCSB], [https://www.ebi.ac.uk/pdbsum/1eoq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eoq ProSAT]</span></td></tr>
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{{STRUCTURE_1eoq| PDB=1eoq | SCENE= }}
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</table>
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== Function ==
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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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eo/1eoq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eoq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: The capsid protein (CA) of retroviruses, such as Rous sarcoma virus (RSV), consists of two independently folded domains. CA functions as part of a polyprotein during particle assembly and budding and, in addition, forms a shell encapsidating the genomic RNA in the mature, infectious virus. RESULTS: The structures of the N- and C-terminal domains of RSV CA have been determined by X-ray crystallography and solution nuclear magnetic resonance (NMR) spectroscopy, respectively. The N-terminal domain comprises seven alpha helices and a short beta hairpin at the N terminus. The N-terminal domain associates through a small, tightly packed, twofold symmetric interface within the crystal, different from those previously described for other retroviral CAs. The C-terminal domain is a compact bundle of four alpha helices, although the last few residues are disordered. In dilute solution, RSV CA is predominantly monomeric. We show, however, using electron microscopy, that intact RSV CA can assemble in vitro to form both tubular structures constructed from toroidal oligomers and planar monolayers. Both modes of assembly occur under similar solution conditions, and both sheets and tubes exhibit long-range order. CONCLUSIONS: The tertiary structure of CA is conserved across the major retroviral genera, yet sequence variations are sufficient to cause change in associative behavior. CA forms the exterior shell of the viral core in all mature retroviruses. However, the core morphology differs between viruses. Consistent with this observation, we find that the capsid proteins of RSV and human immunodeficiency virus type 1 exhibit different associative behavior in dilute solution and assemble in vitro into different structures.
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'''ROUS SARCOMA VIRUS CAPSID PROTEIN: C-TERMINAL DOMAIN'''
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Structure and self-association of the Rous sarcoma virus capsid protein.,Kingston RL, Fitzon-Ostendorp T, Eisenmesser EZ, Schatz GW, Vogt VM, Post CB, Rossmann MG Structure. 2000 Jun 15;8(6):617-28. PMID:10873863<ref>PMID:10873863</ref>
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==Overview==
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BACKGROUND: The capsid protein (CA) of retroviruses, such as Rous sarcoma virus (RSV), consists of two independently folded domains. CA functions as part of a polyprotein during particle assembly and budding and, in addition, forms a shell encapsidating the genomic RNA in the mature, infectious virus. RESULTS: The structures of the N- and C-terminal domains of RSV CA have been determined by X-ray crystallography and solution nuclear magnetic resonance (NMR) spectroscopy, respectively. The N-terminal domain comprises seven alpha helices and a short beta hairpin at the N terminus. The N-terminal domain associates through a small, tightly packed, twofold symmetric interface within the crystal, different from those previously described for other retroviral CAs. The C-terminal domain is a compact bundle of four alpha helices, although the last few residues are disordered. In dilute solution, RSV CA is predominantly monomeric. We show, however, using electron microscopy, that intact RSV CA can assemble in vitro to form both tubular structures constructed from toroidal oligomers and planar monolayers. Both modes of assembly occur under similar solution conditions, and both sheets and tubes exhibit long-range order. CONCLUSIONS: The tertiary structure of CA is conserved across the major retroviral genera, yet sequence variations are sufficient to cause change in associative behavior. CA forms the exterior shell of the viral core in all mature retroviruses. However, the core morphology differs between viruses. Consistent with this observation, we find that the capsid proteins of RSV and human immunodeficiency virus type 1 exhibit different associative behavior in dilute solution and assemble in vitro into different structures.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1EOQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOQ OCA].
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</div>
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<div class="pdbe-citations 1eoq" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structure and self-association of the Rous sarcoma virus capsid protein., Kingston RL, Fitzon-Ostendorp T, Eisenmesser EZ, Schatz GW, Vogt VM, Post CB, Rossmann MG, Structure. 2000 Jun 15;8(6):617-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10873863 10873863]
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*[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]]
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[[Category: Rous sarcoma virus]]
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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[[Category: Single protein]]
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== References ==
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[[Category: Eisenmesser, E Z.]]
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<references/>
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[[Category: Fitzon-Ostendorp, T.]]
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__TOC__
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[[Category: Kingston, R L.]]
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</StructureSection>
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[[Category: Post, C B.]]
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[[Category: Large Structures]]
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[[Category: Rossman, M G.]]
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[[Category: Rous sarcoma virus - Prague C]]
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[[Category: Schatz, G W.]]
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[[Category: Eisenmesser EZ]]
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[[Category: Vogt, V M.]]
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[[Category: Fitzon-Ostendorp T]]
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[[Category: Virus/viral protein]]
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[[Category: Kingston RL]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:21:24 2008''
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[[Category: Post CB]]
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[[Category: Rossmann MG]]
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[[Category: Schatz GW]]
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[[Category: Vogt VM]]

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ROUS SARCOMA VIRUS CAPSID PROTEIN: C-TERMINAL DOMAIN

PDB ID 1eoq

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