2n21: Difference between revisions
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<StructureSection load='2n21' size='340' side='right'caption='[[2n21]]' scene=''> | <StructureSection load='2n21' size='340' side='right'caption='[[2n21]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full | <table><tr><td colspan='2'>[[2n21]] 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 experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N21 FirstGlance]. <br> | ||
</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=2n21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n21 OCA], [https://pdbe.org/2n21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n21 RCSB], [https://www.ebi.ac.uk/pdbsum/2n21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n21 ProSAT]</span></td></tr> | </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=2n21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n21 OCA], [https://pdbe.org/2n21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n21 RCSB], [https://www.ebi.ac.uk/pdbsum/2n21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n21 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DHX36_HUMAN DHX36_HUMAN] Proposed to have a global role in regulating mRNA expression including transcriptional regulation and mRNA stability. Binds with high affinity to and resolves tetramolecular RNA and DNA quadruplex structures. Unwinds intramolecular quadruplexes derived from the ZIC1 and the MYC promoters. Binds to quadruplex structures in the promoters of YY1 and ALPL genes and regulates their expression. Binds to telomerase RNA template component (TERC) 5'-end (nucleotides 1-43) and unwinds an internal quadruplex formation in TERC 5'-end to promote P1 helix formation; the P1 helix acts as a template boundary ensuring accurate reverse transcription and is disrupted by quadruplex formation. May be involved in regulation of telomere length. Plays a role in degradation and deadenylation of mRNAs containing in their 3'-UTR the consensus ARE sequence element. May function in sex development and spermatogenesis. May play a role in ossification.<ref>PMID:12198572</ref> <ref>PMID:14731398</ref> <ref>PMID:16150737</ref> <ref>PMID:18842585</ref> <ref>PMID:20472641</ref> <ref>PMID:21149580</ref> <ref>PMID:21586581</ref> <ref>PMID:21993297</ref> <ref>PMID:22238380</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Four-stranded nucleic acid structures called G-quadruplexes have been associated with important cellular processes, which should require G-quadruplex-protein interaction. However, the structural basis for specific G-quadruplex recognition by proteins has not been understood. The DEAH (Asp-Glu-Ala-His) box RNA helicase associated with AU-rich element (RHAU) (also named DHX36 or G4R1) specifically binds to and resolves parallel-stranded G-quadruplexes. Here we identified an 18-amino acid G-quadruplex-binding domain of RHAU and determined the structure of this peptide bound to a parallel DNA G-quadruplex. Our structure explains how RHAU specifically recognizes parallel G-quadruplexes. The peptide covers a terminal guanine base tetrad (G-tetrad), and clamps the G-quadruplex using three-anchor-point electrostatic interactions between three positively charged amino acids and negatively charged phosphate groups. This binding mode is strikingly similar to that of most ligands selected for specific G-quadruplex targeting. Binding to an exposed G-tetrad represents a simple and efficient way to specifically target G-quadruplex structures. | |||
Insights into G-quadruplex specific recognition by the DEAH-box helicase RHAU: Solution structure of a peptide-quadruplex complex.,Heddi B, Cheong VV, Martadinata H, Phan AT Proc Natl Acad Sci U S A. 2015 Jul 20. pii: 201422605. PMID:26195789<ref>PMID:26195789</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2n21" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Helicase 3D structures|Helicase 3D structures]] | *[[Helicase 3D structures|Helicase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Synthetic construct]] | |||
[[Category: Cheong VV]] | [[Category: Cheong VV]] | ||
[[Category: Heddi B]] | [[Category: Heddi B]] | ||
[[Category: Martadinata H]] | [[Category: Martadinata H]] | ||
[[Category: Phan AT]] | [[Category: Phan AT]] | ||