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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/17070549 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17070549 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17070549 | http://www.w3.org/2000/01/rdf-schema#comment | "The specific binding of HIV-1 nucleocapsid protein (NC) to the different forms assumed in vitro by the stemloop 1 (Lai variant) of the genome's packaging signal has been investigated using electrospray ionization-Fourier transform mass spectrometry (ESI-FTMS). The simultaneous observation of protein-RNA and RNA-RNA interactions in solution has provided direct information about the role of NC in the two-step model of RNA dimerization and isomerization. In particular, two distinct binding sites have been identified on the monomeric stemloop structure, corresponding to the apical loop and stem-bulge motifs. These sites share similar binding affinities that are intermediate between those of stemloop 3 (SL3) and the putative stemloop 4 (SL4) of the packaging signal. Binding to the apical loop, which contains the dimerization initiation site (DIS), competes directly with the annealing of self-complementary sequences to form a metastable kissing-loop (KL) dimer. In contrast, binding to the stem-bulge affects indirectly the monomer-dimer equilibrium by promoting the rearrangement of KL into the more stable extended duplex (ED) conformer. This process is mediated by the duplex-melting activity of NC, which destabilizes the intramolecular base-pairs surrounding the KL stem-bulges and enables their exchange to form the inter-strand pairs that define the ED structure. In this conformer, high-affinity binding takes place at stem-bulge sites that are identical to those present in the monomeric and KL forms. In this case, however, the NC-induced "breathing" does not result in dissociation of the double-stranded structure because of the large number of intermolecular base-pairs. The different binding modes manifested by conformer-specific mutants have shown that NC can also provide low affinity interactions with the bulged-out adenine bases flanking the DIS region of the ED conformer, thus supporting the hypothesis that these exposed nucleotides may constitute "base-grips" for protein contacts during the late stages of the viral lifecycle."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2006.09.081"xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2006.09.081"xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/author | "Fabris D."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/author | "Fabris D."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/author | "Hagan N.A."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/author | "Hagan N.A."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/pages | "396-410"xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/pages | "396-410"xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/title | "Dissecting the protein-RNA and RNA-RNA interactions in the nucleocapsid-mediated dimerization and isomerization of HIV-1 stemloop 1."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/title | "Dissecting the protein-RNA and RNA-RNA interactions in the nucleocapsid-mediated dimerization and isomerization of HIV-1 stemloop 1."xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/volume | "365"xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://purl.uniprot.org/core/volume | "365"xsd:string |
| http://purl.uniprot.org/citations/17070549 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17070549 |
| http://purl.uniprot.org/citations/17070549 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17070549 |
| http://purl.uniprot.org/citations/17070549 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17070549 |
| http://purl.uniprot.org/citations/17070549 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17070549 |
| http://purl.uniprot.org/uniprot/P04585 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17070549 |
| http://purl.uniprot.org/uniprot/P04591 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17070549 |