View source for 6rol


==Structure of IMP2 KH34 domains==
<StructureSection load='6rol' size='340' side='right'caption='[[6rol]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rol]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ROL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ROL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6rol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rol OCA], [https://pdbe.org/6rol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rol RCSB], [https://www.ebi.ac.uk/pdbsum/6rol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rol ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IF2B2_HUMAN IF2B2_HUMAN] Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. May regulate translation of target mRNAs.<ref>PMID:9891060</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The IGF2 mRNA-binding proteins (ZBP1/IMP1, IMP2, IMP3) are highly conserved post-transcriptional regulators of RNA stability, localization and translation. They play important roles in cell migration, neural development, metabolism and cancer cell survival. The knockout phenotypes of individual IMP proteins suggest that each family member regulates a unique pool of RNAs, yet evidence and an underlying mechanism for this is lacking. Here, we combine systematic evolution of ligands by exponential enrichment (SELEX) and NMR spectroscopy to demonstrate that the major RNA-binding domains of the two most distantly related IMPs (ZBP1 and IMP2) bind to different consensus sequences and regulate targets consistent with their knockout phenotypes and roles in disease. We find that the targeting specificity of each IMP is determined by few amino acids in their variable loops. As variable loops often differ amongst KH domain paralogs, we hypothesize that this is a general mechanism for evolving specificity and regulation of the transcriptome.

The structural basis for RNA selectivity by the IMP family of RNA-binding proteins.,Biswas J, Patel VL, Bhaskar V, Chao JA, Singer RH, Eliscovich C Nat Commun. 2019 Sep 30;10(1):4440. doi: 10.1038/s41467-019-12193-7. PMID:31570709<ref>PMID:31570709</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rol" style="background-color:#fffaf0;"></div>

==See Also==
*[[Insulin-like growth factor 2 mRNA-binding protein|Insulin-like growth factor 2 mRNA-binding protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bhaskar V]]
[[Category: Biswas J]]
[[Category: Chao JA]]
[[Category: Singer RH]]