3ulj: Difference between revisions
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[[ | ==Crystal structure of apo Lin28B cold shock domain== | ||
<StructureSection load='3ulj' size='340' side='right' caption='[[3ulj]], [[Resolution|resolution]] 1.06Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ulj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_(silurana)_tropicalis Xenopus (silurana) 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ULJ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lin28b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8364 Xenopus (Silurana) tropicalis])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ulj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ulj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ulj RCSB], [http://www.ebi.ac.uk/pdbsum/3ulj PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Doege, N]] | |||
== | [[Category: Heinemann, U]] | ||
< | [[Category: Mayr, F]] | ||
[[Category: Doege, N | [[Category: Schuetz, A]] | ||
[[Category: Heinemann, U | |||
[[Category: Mayr, F | |||
[[Category: Schuetz, A | |||
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Cold shock domain fold]] | [[Category: Cold shock domain fold]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Nucleic acid binding]] | [[Category: Nucleic acid binding]] | ||
