1m82

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(New page: 200px<br /><applet load="1m82" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m82" /> '''SOLUTION STRUCTURE OF THE COMPLEMENTARY RNA ...)
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[[Image:1m82.gif|left|200px]]<br /><applet load="1m82" size="350" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION STRUCTURE OF THE COMPLEMENTARY RNA PROMOTER OF INFLUENZA A VIRUS'''<br />
'''SOLUTION STRUCTURE OF THE COMPLEMENTARY RNA PROMOTER OF INFLUENZA A VIRUS'''<br />
==Overview==
==Overview==
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Influenza A virus replication requires the interaction of viral, RNA-dependent RNA polymerase (RdRp) with promoters in both the RNA genome, (vRNA) and the full-length complementary RNA (cRNA) which serve as, templates for the generation of new vRNAs. Although RdRp binds both, promoters effectively, it must also discriminate between them because they, serve different functional roles in the viral life cycle. Even though the, inherent asymmetry between two RNA promoters is considered as a cause of, the differential recognition by the RdRp, the structural basis for the, ability of the RdRp to recognize the RNA promoters and discriminate, effectively between them remains unsolved. Here we report the structure of, the cRNA promoter of influenza A virus as determined by heteronuclear, magnetic resonance spectroscopy. The terminal region is extremely unstable, and does not have a rigid structure. The major groove of the internal loop, is widened by the displacement of a novel A*(UU) motif toward the minor, groove. These internal loop residues show distinguishable dynamic, characters, with differing motional timescales for each residue., Comparison of the cRNA promoter structure with that of the vRNA promoter, reveals common structural and dynamic elements in the internal loop, but, also differences that provide insight into how the viral RdRp, differentially recognizes the cRNA and vRNA promoters.
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Influenza A virus replication requires the interaction of viral RNA-dependent RNA polymerase (RdRp) with promoters in both the RNA genome (vRNA) and the full-length complementary RNA (cRNA) which serve as templates for the generation of new vRNAs. Although RdRp binds both promoters effectively, it must also discriminate between them because they serve different functional roles in the viral life cycle. Even though the inherent asymmetry between two RNA promoters is considered as a cause of the differential recognition by the RdRp, the structural basis for the ability of the RdRp to recognize the RNA promoters and discriminate effectively between them remains unsolved. Here we report the structure of the cRNA promoter of influenza A virus as determined by heteronuclear magnetic resonance spectroscopy. The terminal region is extremely unstable and does not have a rigid structure. The major groove of the internal loop is widened by the displacement of a novel A*(UU) motif toward the minor groove. These internal loop residues show distinguishable dynamic characters, with differing motional timescales for each residue. Comparison of the cRNA promoter structure with that of the vRNA promoter reveals common structural and dynamic elements in the internal loop, but also differences that provide insight into how the viral RdRp differentially recognizes the cRNA and vRNA promoters.
==About this Structure==
==About this Structure==
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1M82 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M82 OCA].
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1M82 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M82 OCA].
==Reference==
==Reference==
Solution structure of the influenza A virus cRNA promoter: implications for differential recognition of viral promoter structures by RNA-dependent RNA polymerase., Park CJ, Bae SH, Lee MK, Varani G, Choi BS, Nucleic Acids Res. 2003 Jun 1;31(11):2824-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12771209 12771209]
Solution structure of the influenza A virus cRNA promoter: implications for differential recognition of viral promoter structures by RNA-dependent RNA polymerase., Park CJ, Bae SH, Lee MK, Varani G, Choi BS, Nucleic Acids Res. 2003 Jun 1;31(11):2824-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12771209 12771209]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Bae, S.H.]]
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[[Category: Bae, S H.]]
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[[Category: Choi, B.S.]]
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[[Category: Choi, B S.]]
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[[Category: Lee, M.K.]]
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[[Category: Lee, M K.]]
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[[Category: Park, C.J.]]
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[[Category: Park, C J.]]
[[Category: Varani, G.]]
[[Category: Varani, G.]]
[[Category: a-form helix]]
[[Category: a-form helix]]
[[Category: asymmetric internal loop]]
[[Category: asymmetric internal loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:55:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:30 2008''

Revision as of 11:52, 21 February 2008


1m82

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SOLUTION STRUCTURE OF THE COMPLEMENTARY RNA PROMOTER OF INFLUENZA A VIRUS

Overview

Influenza A virus replication requires the interaction of viral RNA-dependent RNA polymerase (RdRp) with promoters in both the RNA genome (vRNA) and the full-length complementary RNA (cRNA) which serve as templates for the generation of new vRNAs. Although RdRp binds both promoters effectively, it must also discriminate between them because they serve different functional roles in the viral life cycle. Even though the inherent asymmetry between two RNA promoters is considered as a cause of the differential recognition by the RdRp, the structural basis for the ability of the RdRp to recognize the RNA promoters and discriminate effectively between them remains unsolved. Here we report the structure of the cRNA promoter of influenza A virus as determined by heteronuclear magnetic resonance spectroscopy. The terminal region is extremely unstable and does not have a rigid structure. The major groove of the internal loop is widened by the displacement of a novel A*(UU) motif toward the minor groove. These internal loop residues show distinguishable dynamic characters, with differing motional timescales for each residue. Comparison of the cRNA promoter structure with that of the vRNA promoter reveals common structural and dynamic elements in the internal loop, but also differences that provide insight into how the viral RdRp differentially recognizes the cRNA and vRNA promoters.

About this Structure

1M82 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Solution structure of the influenza A virus cRNA promoter: implications for differential recognition of viral promoter structures by RNA-dependent RNA polymerase., Park CJ, Bae SH, Lee MK, Varani G, Choi BS, Nucleic Acids Res. 2003 Jun 1;31(11):2824-32. PMID:12771209

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