4c7q: Difference between revisions

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New page: {{STRUCTURE_4c7q| PDB=4c7q | SCENE= }} ===Solution structure of the Nt. GR-RBP1 RRM domain=== ==About this Structure== 4c7q is a 1 chain structure with sequence from [http://en.w...
 
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{{STRUCTURE_4c7q|  PDB=4c7q  |  SCENE=  }}
===Solution structure of the Nt. GR-RBP1 RRM domain===


==About this Structure==
==Solution structure of the Nt. GR-RBP1 RRM domain==
[[4c7q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7Q OCA].  
<StructureSection load='4c7q' size='340' side='right'caption='[[4c7q]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4c7q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C7Q 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=4c7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7q OCA], [https://pdbe.org/4c7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c7q RCSB], [https://www.ebi.ac.uk/pdbsum/4c7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7q ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D6PZY5_TOBAC D6PZY5_TOBAC]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycine-rich RNA-binding proteins (GR-RBPs) are involved in cold shock response of plants as RNA chaperones facilitating mRNA transport, splicing and translation. GR-RBPs are bipartite proteins containing a RNA recognition motif (RRM) followed by a glycine-rich region. Here, we studied the structural basis of nucleic acid binding of full-length Nicotiana tabacum GR-RBP1. NMR studies of NtGR-RBP1 show that the glycine-rich domain, while intrinsically disordered, is responsible for mediating self-association by transient interactions with its RRM domain (NtRRM). Both NtGR-RBP1 and NtRRM bind specifically and with low micromolar affinity to RNA and single-stranded DNA. The solution structure of NtRRM shows that it is a canonical RRM domain. A HADDOCK model of the NtRRM-RNA complex, based on NMR chemical shift and NOE data, shows that nucleic acid binding results from a combination of stacking and electrostatic interactions with conserved RRM residues. Finally, DNA melting experiments demonstrate that NtGR-RBP1 is more efficient in melting CTG containing nucleic acids than isolated NtRRM. Together, our study supports the model that self-association of GR-RBPs by the glycine-rich region results in cooperative unfolding of non-native substrate structures, thereby enhancing its chaperone function.
 
Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function.,Khan F, Daniels MA, Folkers GE, Boelens R, Saqlan Naqvi SM, Ingen HV Nucleic Acids Res. 2014 Jun 23. pii: gku468. PMID:24957607<ref>PMID:24957607</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4c7q" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Nicotiana tabacum]]
[[Category: Nicotiana tabacum]]
[[Category: Boelens, R.]]
[[Category: Boelens R]]
[[Category: Ingen, H van.]]
[[Category: Kahn F]]
[[Category: Kahn, F.]]
[[Category: Saqlan SMS]]
[[Category: Saqlan, S M.]]
[[Category: Van Ingen H]]
[[Category: Rna binding protein]]

Latest revision as of 06:00, 19 June 2024

Solution structure of the Nt. GR-RBP1 RRM domain

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