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==Crystal structure of ATP-dependent RNA helicase DDX42== | ==Crystal structure of ATP-dependent RNA helicase DDX42== | ||
<StructureSection load='8dpe' size='340' side='right'caption='[[8dpe]]' scene=''> | <StructureSection load='8dpe' size='340' side='right'caption='[[8dpe]], [[Resolution|resolution]] 1.53Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DPE FirstGlance]. <br> | <table><tr><td colspan='2'>[[8dpe]] is a 1 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=8DPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DPE 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=8dpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dpe OCA], [https://pdbe.org/8dpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dpe RCSB], [https://www.ebi.ac.uk/pdbsum/8dpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dpe ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.531Å</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=8dpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dpe OCA], [https://pdbe.org/8dpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dpe RCSB], [https://www.ebi.ac.uk/pdbsum/8dpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dpe ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DDX42_HUMAN DDX42_HUMAN] ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm.<ref>PMID:16397294</ref> <ref>PMID:19377511</ref> | |||
==See Also== | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Larsen NA]] | [[Category: Larsen NA]] | ||
[[Category: Tsai J]] | [[Category: Tsai J]] | ||
Latest revision as of 20:29, 18 October 2023
Crystal structure of ATP-dependent RNA helicase DDX42Crystal structure of ATP-dependent RNA helicase DDX42
Structural highlights
FunctionDDX42_HUMAN ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm.[1] [2] See AlsoReferences
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