1d1d

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(New page: 200px<br /><applet load="1d1d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d1d" /> '''NMR SOLUTION STRUCTURE OF THE CAPSID PROTEIN...)
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[[Image:1d1d.gif|left|200px]]<br /><applet load="1d1d" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d1d" />
 
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'''NMR SOLUTION STRUCTURE OF THE CAPSID PROTEIN FROM ROUS SARCOMA VIRUS'''<br />
 
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==Overview==
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==NMR SOLUTION STRUCTURE OF THE CAPSID PROTEIN FROM ROUS SARCOMA VIRUS==
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The solution structure and dynamics of the recombinant 240 amino acid, residue capsid protein from the Rous sarcoma virus has been determined by, NMR methods. The structure was determined using 2200 distance restraints, and 330 torsion angle restraints, and the dynamics analysis was based on, (15)N relaxation parameters (R(1), R(2), and (1)H-(15)N NOE) measured for, 153 backbone amide groups. The monomeric protein consists of independently, folded N- and C-terminal domains that comprise residues Leu14-Leu146 and, Ala150-Gln226, respectively. The domains exhibit different rotational, correlation times (16.6(+/-0.1) ns and 12.6(+/-0.1) ns, respectively), are, connected by a flexible linker (Ala147-Pro149), and do not give rise to, inter-domain NOE values, indicating that they are dynamically independent., Despite limited sequence similarity, the structure of the Rous sarcoma, virus capsid protein is similar to the structures determined recently for, the capsid proteins of retroviruses belonging to the lentivirus and human, T-cell leukemia virus/bovine leukemia virus genera. Structural differences, that exist in the C-terminal domain of Rous sarcoma virus capsid relative, to the other capsid proteins appear to be related to the occurrence of, conserved cysteine residues. Whereas most genera of retroviruses contain a, pair of conserved and essential cysteine residues in the C-terminal domain, that appear to function by forming an intramolecular disulfide bond during, assembly, the Rous sarcoma virus capsid protein does not. Instead, the, Rous sarcoma virus capsid protein contains a single cysteine residue that, appears to be conserved among the avian C-type retroviruses and is, positioned in a manner that might allow the formation of an intermolecular, disulfide bond during capsid assembly.
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<StructureSection load='1d1d' size='340' side='right'caption='[[1d1d]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d1d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D1D FirstGlance]. <br>
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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=1d1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1d OCA], [https://pdbe.org/1d1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d1d RCSB], [https://www.ebi.ac.uk/pdbsum/1d1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d1d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GAG_RSVSB GAG_RSVSB] 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/d1/1d1d_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=1d1d 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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The solution structure and dynamics of the recombinant 240 amino acid residue capsid protein from the Rous sarcoma virus has been determined by NMR methods. The structure was determined using 2200 distance restraints and 330 torsion angle restraints, and the dynamics analysis was based on (15)N relaxation parameters (R(1), R(2), and (1)H-(15)N NOE) measured for 153 backbone amide groups. The monomeric protein consists of independently folded N- and C-terminal domains that comprise residues Leu14-Leu146 and Ala150-Gln226, respectively. The domains exhibit different rotational correlation times (16.6(+/-0.1) ns and 12.6(+/-0.1) ns, respectively), are connected by a flexible linker (Ala147-Pro149), and do not give rise to inter-domain NOE values, indicating that they are dynamically independent. Despite limited sequence similarity, the structure of the Rous sarcoma virus capsid protein is similar to the structures determined recently for the capsid proteins of retroviruses belonging to the lentivirus and human T-cell leukemia virus/bovine leukemia virus genera. Structural differences that exist in the C-terminal domain of Rous sarcoma virus capsid relative to the other capsid proteins appear to be related to the occurrence of conserved cysteine residues. Whereas most genera of retroviruses contain a pair of conserved and essential cysteine residues in the C-terminal domain that appear to function by forming an intramolecular disulfide bond during assembly, the Rous sarcoma virus capsid protein does not. Instead, the Rous sarcoma virus capsid protein contains a single cysteine residue that appears to be conserved among the avian C-type retroviruses and is positioned in a manner that might allow the formation of an intermolecular disulfide bond during capsid assembly.
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==About this Structure==
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Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses.,Campos-Olivas R, Newman JL, Summers MF J Mol Biol. 2000 Feb 18;296(2):633-49. PMID:10669613<ref>PMID:10669613</ref>
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1D1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D1D OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses., Campos-Olivas R, Newman JL, Summers MF, J Mol Biol. 2000 Feb 18;296(2):633-49. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10669613 10669613]
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</div>
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[[Category: Rous sarcoma virus]]
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<div class="pdbe-citations 1d1d" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Campos-Olivas, R.]]
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[[Category: Newman, J.L.]]
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[[Category: Summers, M.F.]]
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[[Category: two independent domains helical bundles]]
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[[Category: virus/viral protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:15:08 2007''
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Rous sarcoma virus]]
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[[Category: Campos-Olivas R]]
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[[Category: Newman JL]]
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[[Category: Summers MF]]

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NMR SOLUTION STRUCTURE OF THE CAPSID PROTEIN FROM ROUS SARCOMA VIRUS

PDB ID 1d1d

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