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1d1d

From Proteopedia

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[[Image:1d1d.gif|left|200px]]
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{{Seed}}
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[[Image:1d1d.png|left|200px]]
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{{STRUCTURE_1d1d| PDB=1d1d | SCENE= }}
{{STRUCTURE_1d1d| PDB=1d1d | SCENE= }}
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'''NMR SOLUTION STRUCTURE OF THE CAPSID PROTEIN FROM ROUS SARCOMA VIRUS'''
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===NMR SOLUTION STRUCTURE OF THE CAPSID PROTEIN FROM ROUS SARCOMA VIRUS===
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==Overview==
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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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The line below this paragraph, {{ABSTRACT_PUBMED_10669613}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10669613 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10669613}}
==About this Structure==
==About this Structure==
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1D1D 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=1D1D OCA].
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1D1D is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
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[[Category: Two independent domains helical bundle]]
[[Category: Two independent domains helical bundle]]
[[Category: Virus/viral protein]]
[[Category: Virus/viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:20:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:03:29 2008''

Revision as of 19:03, 30 June 2008

Image:1d1d.png

Template:STRUCTURE 1d1d

NMR SOLUTION STRUCTURE OF THE CAPSID PROTEIN FROM ROUS SARCOMA VIRUS

Template:ABSTRACT PUBMED 10669613

About this Structure

1D1D is a Single protein structure of sequence from Rous sarcoma virus. Full experimental information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jun 30 22:03:29 2008

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