2n21: Difference between revisions

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==Solution structure of complex between DNA G-quadruplex and G-quadruplex recognition domain of RHAU==
==Solution structure of complex between DNA G-quadruplex and G-quadruplex recognition domain of RHAU==
<StructureSection load='2n21' size='340' side='right' caption='[[2n21]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2n21' size='340' side='right'caption='[[2n21]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2n21]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N21 FirstGlance]. <br>
<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n21 OCA], [http://pdbe.org/2n21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n21 RCSB], [http://www.ebi.ac.uk/pdbsum/2n21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n21 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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 ==
== Function ==
[[http://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>
[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>  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cheong, V V]]
[[Category: Homo sapiens]]
[[Category: Heddi, B]]
[[Category: Large Structures]]
[[Category: Martadinata, H]]
[[Category: Synthetic construct]]
[[Category: Phan, A T]]
[[Category: Cheong VV]]
[[Category: Hydrolase-dna complex]]
[[Category: Heddi B]]
[[Category: Martadinata H]]
[[Category: Phan AT]]

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