3ulj: Difference between revisions

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<StructureSection load='3ulj' size='340' side='right'caption='[[3ulj]], [[Resolution|resolution]] 1.06&Aring;' scene=''>
<StructureSection load='3ulj' size='340' side='right'caption='[[3ulj]], [[Resolution|resolution]] 1.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ulj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Silurana_(xenopus)_tropicalis Silurana (xenopus) tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ULJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ULJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ulj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ULJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ULJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.06&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lin28b ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8364 Silurana (Xenopus) tropicalis])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3ulj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ulj OCA], [https://pdbe.org/3ulj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ulj RCSB], [https://www.ebi.ac.uk/pdbsum/3ulj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ulj ProSAT]</span></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=3ulj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ulj OCA], [https://pdbe.org/3ulj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ulj RCSB], [https://www.ebi.ac.uk/pdbsum/3ulj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ulj ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/B4F6I0_XENTR B4F6I0_XENTR]
The RNA-binding protein Lin28 regulates the processing of a developmentally important group of microRNAs, the let-7 family. Lin28 blocks the biogenesis of let-7 in embryonic stem cells and thereby prevents differentiation. It was shown that both RNA-binding domains (RBDs) of this protein, the cold-shock domain (CSD) and the zinc-knuckle domain (ZKD) are indispensable for pri- or pre-let-7 binding and blocking its maturation. Here, we systematically examined the nucleic acid-binding preferences of the Lin28 RBDs and determined the crystal structure of the Lin28 CSD in the absence and presence of nucleic acids. Both RNA-binding domains bind to single-stranded nucleic acids with the ZKD mediating specific binding to a conserved GGAG motif and the CSD showing only limited sequence specificity. However, only the isolated Lin28 CSD, but not the ZKD, can bind with a reasonable affinity to pre-let-7 and thus is able to remodel the terminal loop of pre-let-7 including the Dicer cleavage site. Further mutagenesis studies reveal that the Lin28 CSD induces a conformational change in the terminal loop of pre-let-7 and thereby facilitates a subsequent specific binding of the Lin28 ZKD to the conserved GGAG motif.
 
The Lin28 cold-shock domain remodels pre-let-7 microRNA.,Mayr F, Schutz A, Doge N, Heinemann U Nucleic Acids Res. 2012 May 8. PMID:22570413<ref>PMID:22570413</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ulj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Doege, N]]
[[Category: Xenopus tropicalis]]
[[Category: Heinemann, U]]
[[Category: Doege N]]
[[Category: Mayr, F]]
[[Category: Heinemann U]]
[[Category: Schuetz, A]]
[[Category: Mayr F]]
[[Category: Beta barrel]]
[[Category: Schuetz A]]
[[Category: Cold shock domain fold]]
[[Category: Dna binding protein]]
[[Category: Nucleic acid binding]]
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