2n16

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'''Unreleased structure'''
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==Solution structure of the N-terminal domain of RHAU==
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<StructureSection load='2n16' size='340' side='right' caption='[[2n16]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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The entry 2n16 is ON HOLD
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n16]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N16 FirstGlance]. <br>
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Authors: Heddi, B., Cheong, V.V.V., Martadinata, H., Phan, A.A.T.
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</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=2n16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n16 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2n16 RCSB], [http://www.ebi.ac.uk/pdbsum/2n16 PDBsum]</span></td></tr>
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</table>
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Description: Structure of a peptide
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== Function ==
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[[Category: Unreleased Structures]]
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cheong, V V]]
[[Category: Heddi, B]]
[[Category: Heddi, B]]
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[[Category: Phan, A.A.T]]
 
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[[Category: Cheong, V.V.V]]
 
[[Category: Martadinata, H]]
[[Category: Martadinata, H]]
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[[Category: Phan, A T]]
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[[Category: Hydrolase]]

Revision as of 14:45, 29 July 2015

Solution structure of the N-terminal domain of RHAU

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