2ldl

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[[Image:2ldl.png|left|200px]]
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==Solution NMR Structure of the HIV-1 Exon Splicing Silencer 3==
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<StructureSection load='2ldl' size='340' side='right' caption='[[2ldl]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''>
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== Structural highlights ==
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[[2ldl]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDL OCA]. <br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Publication Abstract from PubMed ==
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Alternative splicing of the human immunodeficiency virus type 1 (HIV-1) genomic RNA is necessary to produce the complete viral protein complement, and aberrations in the splicing pattern impair HIV-1 replication. Genome splicing in HIV-1 is tightly regulated by the dynamic assembly/disassembly of trans host factors with cis RNA control elements. The host protein, heterogeneous nuclear ribonucleoprotein (hnRNP) A1, regulates splicing at several highly conserved HIV-1 3' splice sites by binding 5'-UAG-3' elements embedded within regions containing RNA structure. The physical determinants of hnRNP A1 splice site recognition remain poorly defined in HIV-1, thus precluding a detailed understanding of the molecular basis of the splicing pattern. Here, the three-dimensional structure of the exon splicing silencer 3 (ESS3) from HIV-1 has been determined using NMR spectroscopy. ESS3 adopts a 27-nucleotide hairpin with a 10-bp A-form stem that contains a pH-sensitive A(+)C wobble pair. The seven-nucleotide hairpin loop contains the high-affinity hnRNP-A1-responsive 5'-UAGU-3' element and a proximal 5'-GAU-3' motif. The NMR structure shows that the heptaloop adopts a well-organized conformation stabilized primarily by base stacking interactions reminiscent of a U-turn. The apex of the loop is quasi-symmetric with UA dinucleotide steps from the 5'-GAU-3' and 5'-UAGU-3' motifs stacking on opposite sides of the hairpin. As a step towards understanding the binding mechanism, we performed calorimetric and NMR titrations of several hnRNP A1 subdomains into ESS3. The data show that the UP1 domain forms a high-affinity (K(d)=37.8+/-1.1 nM) complex with ESS3 via site-specific interactions with the loop.
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Solution Structure of the HIV-1 Exon Splicing Silencer 3.,Levengood JD, Rollins C, Mishler CH, Johnson CA, Miner G, Rajan P, Znosko BM, Tolbert BS J Mol Biol. 2011 Nov 29. PMID:22154809<ref>PMID:22154809</ref>
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The line below this paragraph, containing "STRUCTURE_2ldl", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2ldl| PDB=2ldl | SCENE= }}
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===Solution NMR Structure of the HIV-1 Exon Splicing Silencer 3===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_22154809}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 22154809 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22154809}}
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==About this Structure==
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[[2ldl]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDL OCA].
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==Reference==
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<ref group="xtra">PMID:022154809</ref><references group="xtra"/>
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[[Category: Johnson, C A.]]
[[Category: Johnson, C A.]]
[[Category: Levengood, J D.]]
[[Category: Levengood, J D.]]

Revision as of 08:26, 30 April 2014

Solution NMR Structure of the HIV-1 Exon Splicing Silencer 3

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