1m5l: Difference between revisions

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[[Image:1m5l.png|left|200px]]
==Structure of wild-type and mutant internal loops from the SL-1 domain of the HIV-1 packaging signal==
<StructureSection load='1m5l' size='340' side='right' caption='[[1m5l]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m5l]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M5L FirstGlance]. <br>
</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=1m5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m5l RCSB], [http://www.ebi.ac.uk/pdbsum/1m5l PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The packaging signal (Psi) of the human immunodeficiency virus type 1 (HIV-1) enables encapsidation of the full-length genomic RNA against a background of a vast excess of cellular mRNAs. The core HIV-1 Psi is approximately 109 nucleotides and contains sequences critical for viral genomic dimerisation and splicing, in addition to the packaging signal. It consists of a series of stem-loops (termed SL-1 to SL-4), which can be arranged in a cloverleaf secondary structure. Using a combination of NMR spectroscopy, UV melting experiments, molecular modeling and phylogenetic analyses, we have explored the structure of two conserved internal loops proximal to the palindromic sequence of SL-1. Internal loop A, composed of six purines, forms a flexible structure that is strikingly similar to the Rev responsive element motif when bound to Rev protein. This result suggests that it may function as a protein-binding site. The absolutely conserved four-purine internal loop B is instead conformationally and thermodynamically unstable, and exhibits multiple conformations in solution. By introducing a double AGG to GGA mutation within this loop, its conformation is stabilised to form a new intra-molecular G:A:G base-triplet. The structure of the GGA mutant explains the relative instability of the wild-type loop. In a manner analogous to SL-3, we propose that conformational flexibility at this site may facilitate melting of the structure during Gag protein capture or genomic RNA dimerisation.


{{STRUCTURE_1m5l|  PDB=1m5l  |  SCENE=  }}
Structure and stability of wild-type and mutant RNA internal loops from the SL-1 domain of the HIV-1 packaging signal.,Greatorex J, Gallego J, Varani G, Lever A J Mol Biol. 2002 Sep 20;322(3):543-57. PMID:12225748<ref>PMID:12225748</ref>


===Structure of wild-type and mutant internal loops from the SL-1 domain of the HIV-1 packaging signal===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_12225748}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1m5l]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5L OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:012225748</ref><references group="xtra"/>
[[Category: Gallego, J.]]
[[Category: Gallego, J.]]
[[Category: Greatorex, J.]]
[[Category: Greatorex, J.]]

Revision as of 05:28, 8 June 2014

Structure of wild-type and mutant internal loops from the SL-1 domain of the HIV-1 packaging signal

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