5yki: Difference between revisions
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==Crystal structure of the engineered nine-repeat PUF domain in complex with cognate 9nt-RNA== | ==Crystal structure of the engineered nine-repeat PUF domain in complex with cognate 9nt-RNA== | ||
<StructureSection load='5yki' size='340' side='right' caption='[[5yki]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='5yki' size='340' side='right'caption='[[5yki]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5yki]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YKI OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5yki]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YKI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YKI FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yki OCA], [https://pdbe.org/5yki PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yki RCSB], [https://www.ebi.ac.uk/pdbsum/5yki PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yki ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PUM1_HUMAN PUM1_HUMAN] Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Li HT]] | ||
[[Category: | [[Category: Wang J]] | ||
[[Category: | [[Category: Wang ZX]] | ||
[[Category: | [[Category: Wu JW]] | ||
[[Category: | [[Category: Zhao YY]] | ||
Latest revision as of 11:32, 22 November 2023
Crystal structure of the engineered nine-repeat PUF domain in complex with cognate 9nt-RNACrystal structure of the engineered nine-repeat PUF domain in complex with cognate 9nt-RNA
Structural highlights
FunctionPUM1_HUMAN Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity). Publication Abstract from PubMedSpecific manipulation of RNA is necessary for the research in biotechnology and medicine. The RNA-binding domains of Pumilio/fem-3 mRNA binding factors (PUF domains) are programmable RNA binding scaffolds used to engineer artificial proteins that specifically modulate RNAs. However, the native PUF domains generally recognize 8-nt RNAs, limiting their applications. Here, we modify the PUF domain of human Pumilio1 to engineer PUFs that recognize RNA targets of different length. The engineered PUFs bind to their RNA targets specifically and PUFs with more repeats have higher binding affinity than the canonical eight-repeat domains; however, the binding affinity reaches the peak at those with 9 and 10 repeats. Structural analysis on PUF with nine repeats reveals a higher degree of curvature, and the RNA binding unexpectedly and dramatically opens the curved structure. Investigation of the residues positioned in between two RNA bases demonstrates that tyrosine and arginine have favored stacking interactions. Further tests on the availability of the engineered PUFs in vitro and in splicing function assays indicate that our engineered PUFs bind RNA targets with high affinity in a programmable way. Expanding RNA binding specificity and affinity of engineered PUF domains.,Zhao YY, Mao MW, Zhang WJ, Wang J, Li HT, Yang Y, Wang Z, Wu JW Nucleic Acids Res. 2018 Feb 27. pii: 4911549. doi: 10.1093/nar/gky134. PMID:29490074[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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