1rfr: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1rfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rfr" /> '''NMR structure of the 30mer stemloop-D of cox...
 
OCA (talk | contribs)
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1rfr.gif|left|200px]]<br /><applet load="1rfr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rfr" />
'''NMR structure of the 30mer stemloop-D of coxsackieviral RNA'''<br />


==Overview==
==NMR structure of the 30mer stemloop-D of coxsackieviral RNA==
Stemloop D (SLD) of the 5' cloverleaf RNA is the cognate ligand of the, coxsackievirus B3 (CVB3) 3C proteinase (3Cpro). Both are indispensable, components of the viral replication initiation complex. SLD is a, structurally autonomous subunit of the 5' cloverleaf. The SLD structure, was solved by NMR spectroscopy to an rms deviation of 0.66 A (all heavy, atoms). SLD contains a novel triple pyrimidine mismatch motif with a, central Watson-Crick type C:U pair. SLD is capped by an apical uCACGg, tetraloop adopting a structure highly similar to stable cUNCGg tetraloops., Binding of CVB3 3Cpro induces changes in NMR spectra for nucleotides, adjacent to the triple pyrimidine mismatch and of the tetraloop implying, them as sites of specific SLD:3Cpro interaction. The binding of 3Cpro to, SLD requires the integrity of those structural elements, strongly, suggesting that 3Cpro recognizes a structural motif instead of a specific, sequence.
<StructureSection load='1rfr' size='340' side='right'caption='[[1rfr]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coxsackievirus_B3 Coxsackievirus B3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RFR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rfr OCA], [https://pdbe.org/1rfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rfr RCSB], [https://www.ebi.ac.uk/pdbsum/1rfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rfr ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Stemloop D (SLD) of the 5' cloverleaf RNA is the cognate ligand of the coxsackievirus B3 (CVB3) 3C proteinase (3Cpro). Both are indispensable components of the viral replication initiation complex. SLD is a structurally autonomous subunit of the 5' cloverleaf. The SLD structure was solved by NMR spectroscopy to an rms deviation of 0.66 A (all heavy atoms). SLD contains a novel triple pyrimidine mismatch motif with a central Watson-Crick type C:U pair. SLD is capped by an apical uCACGg tetraloop adopting a structure highly similar to stable cUNCGg tetraloops. Binding of CVB3 3Cpro induces changes in NMR spectra for nucleotides adjacent to the triple pyrimidine mismatch and of the tetraloop implying them as sites of specific SLD:3Cpro interaction. The binding of 3Cpro to SLD requires the integrity of those structural elements, strongly suggesting that 3Cpro recognizes a structural motif instead of a specific sequence.


==About this Structure==
The structure of the stemloop D subdomain of coxsackievirus B3 cloverleaf RNA and its interaction with the proteinase 3C.,Ohlenschlager O, Wohnert J, Bucci E, Seitz S, Hafner S, Ramachandran R, Zell R, Gorlach M Structure. 2004 Feb;12(2):237-48. PMID:14962384<ref>PMID:14962384</ref>
1RFR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_coxsackievirus_b1 Human coxsackievirus b1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RFR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The structure of the stemloop D subdomain of coxsackievirus B3 cloverleaf RNA and its interaction with the proteinase 3C., Ohlenschlager O, Wohnert J, Bucci E, Seitz S, Hafner S, Ramachandran R, Zell R, Gorlach M, Structure. 2004 Feb;12(2):237-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14962384 14962384]
</div>
[[Category: Human coxsackievirus b1]]
<div class="pdbe-citations 1rfr" style="background-color:#fffaf0;"></div>
[[Category: Protein complex]]
== References ==
[[Category: Bucci, E.]]
<references/>
[[Category: Gorlach, M.]]
__TOC__
[[Category: Hafner, S.]]
</StructureSection>
[[Category: Ohlenschlager, O.]]
[[Category: Coxsackievirus B3]]
[[Category: Ramachandran, R.]]
[[Category: Large Structures]]
[[Category: Seitz, S.]]
[[Category: Bucci E]]
[[Category: Wohnert, J.]]
[[Category: Gorlach M]]
[[Category: Zell, R.]]
[[Category: Hafner S]]
[[Category: a-form helix stems]]
[[Category: Ohlenschlager O]]
[[Category: base-paired u:u-c:u-u:u mismatch]]
[[Category: Ramachandran R]]
[[Category: loop with conformation similar to stable uncg-tetraloops and u:g closing base pair]]
[[Category: Seitz S]]
 
[[Category: Wohnert J]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:37:34 2007''
[[Category: Zell R]]

Latest revision as of 09:21, 6 December 2023

NMR structure of the 30mer stemloop-D of coxsackieviral RNA

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA