1s2f

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[[Image:1s2f.png|left|200px]]
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==Average solution structure of a pseudo-5'-splice site from the negative regulator of splicing of Rous Sarcoma virus==
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<StructureSection load='1s2f' size='340' side='right' caption='[[1s2f]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1s2f]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S2F FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1s2f RCSB], [http://www.ebi.ac.uk/pdbsum/1s2f PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Control of Rous sarcoma virus RNA splicing depends in part on the interaction of U1 and U11 snRNPs with an intronic RNA element called the negative regulator of splicing (NRS). A 23mer RNA hairpin (NRS23) of the NRS directly binds U1 and U11 snRNPs. Mutations that disrupt base-pairing between the loop of NRS23 and U1 snRNA abolish its negative control of splicing. We have determined the solution structure of NRS23 using NOEs, torsion angles, and residual dipolar couplings that were extracted from multidimensional heteronuclear NMR spectra. Our structure showed that the 6-bp stem of NRS23 adopts a nearly A-form duplex conformation. The loop, which consists of 11 residues according to secondary structure probing, was in a closed conformation. U913, the first residue in the loop, was bulged out or dynamic, and loop residues G914-C923, G915-U922, and U916-A921 were base-paired. The remaining UUGU tetraloop sequence did not adopt a stable structure and appears flexible in solution. This tetraloop differs from the well-known classes of tetraloops (GNRA, CUYG, UNCG) in terms of its stability, structure, and function. Deletion of the bulged U913, which is not complementary to U1 snRNA, increased the melting temperature of the RNA hairpin. This hyperstable hairpin exhibited a significant decrease in binding to U1 snRNP. Thus, the structure of the NRS RNA, as well as its sequence, is important for interaction with U1 snRNP and for splicing suppression.
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{{STRUCTURE_1s2f| PDB=1s2f | SCENE= }}
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Solution structure of the pseudo-5' splice site of a retroviral splicing suppressor.,Cabello-Villegas J, Giles KE, Soto AM, Yu P, Mougin A, Beemon KL, Wang YX RNA. 2004 Sep;10(9):1388-98. PMID:15317975<ref>PMID:15317975</ref>
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===Average solution structure of a pseudo-5'-splice site from the negative regulator of splicing of Rous Sarcoma virus===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_15317975}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1s2f]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2F OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:015317975</ref><references group="xtra"/>
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[[Category: Beemon, K L.]]
[[Category: Beemon, K L.]]
[[Category: Cabello-Villegas, J.]]
[[Category: Cabello-Villegas, J.]]

Revision as of 06:49, 9 June 2014

Average solution structure of a pseudo-5'-splice site from the negative regulator of splicing of Rous Sarcoma virus

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