1p5o
From Proteopedia
(New page: 200px<br /><applet load="1p5o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p5o" /> '''Solution Structure of HCV IRES Domain II'''<...) |
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| - | [[Image:1p5o.gif|left|200px]]<br /><applet load="1p5o" size=" | + | [[Image:1p5o.gif|left|200px]]<br /><applet load="1p5o" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of HCV IRES Domain II'''<br /> | '''Solution Structure of HCV IRES Domain II'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Complex RNA structures regulate many biological processes, but are often | + | Complex RNA structures regulate many biological processes, but are often too large for structure determination by NMR methods. The 5' untranslated region (5' UTR) of the hepatitis C viral (HCV) RNA genome contains an internal ribosome entry site (IRES) that binds to 40S ribosomal subunits with high affinity and specificity to control translation. Domain II of the HCV IRES forms a 25-kDa folded subdomain that may alter ribosome conformation. We report here the structure of domain II as determined using an NMR approach that combines short- and long-range structural data. Domain II adopts a distorted L-shape structure, and its overall shape in the free form is markedly similar to its 40S subunit-bound form; this suggests how domain II may modulate 40S subunit conformation. The results show how NMR can be used for structural analysis of large biological RNAs. |
==About this Structure== | ==About this Structure== | ||
| - | 1P5O 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:// | + | 1P5O 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=1P5O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Kim, I.]] | [[Category: Kim, I.]] | ||
| - | [[Category: Lukavsky, P | + | [[Category: Lukavsky, P J.]] |
| - | [[Category: Otto, G | + | [[Category: Otto, G A.]] |
| - | [[Category: Puglisi, J | + | [[Category: Puglisi, J D.]] |
[[Category: hairpin loop]] | [[Category: hairpin loop]] | ||
[[Category: hepatitis c virus]] | [[Category: hepatitis c virus]] | ||
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[[Category: trna]] | [[Category: trna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:21 2008'' |
Revision as of 12:25, 21 February 2008
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Solution Structure of HCV IRES Domain II
Overview
Complex RNA structures regulate many biological processes, but are often too large for structure determination by NMR methods. The 5' untranslated region (5' UTR) of the hepatitis C viral (HCV) RNA genome contains an internal ribosome entry site (IRES) that binds to 40S ribosomal subunits with high affinity and specificity to control translation. Domain II of the HCV IRES forms a 25-kDa folded subdomain that may alter ribosome conformation. We report here the structure of domain II as determined using an NMR approach that combines short- and long-range structural data. Domain II adopts a distorted L-shape structure, and its overall shape in the free form is markedly similar to its 40S subunit-bound form; this suggests how domain II may modulate 40S subunit conformation. The results show how NMR can be used for structural analysis of large biological RNAs.
About this Structure
1P5O is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structure of HCV IRES domain II determined by NMR., Lukavsky PJ, Kim I, Otto GA, Puglisi JD, Nat Struct Biol. 2003 Dec;10(12):1033-8. Epub 2003 Oct 26. PMID:14578934
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