4a4d: Difference between revisions

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<StructureSection load='4a4d' size='340' side='right'caption='[[4a4d]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='4a4d' size='340' side='right'caption='[[4a4d]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4a4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A4D FirstGlance]. <br>
<table><tr><td colspan='2'>[[4a4d]] 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=4A4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A4D FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </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]] 2.7&#8491;</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=4a4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4d OCA], [https://pdbe.org/4a4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4d RCSB], [https://www.ebi.ac.uk/pdbsum/4a4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4d ProSAT]</span></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=4a4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4d OCA], [https://pdbe.org/4a4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4d RCSB], [https://www.ebi.ac.uk/pdbsum/4a4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DDX5_HUMAN DDX5_HUMAN]] Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation and ESR1 AF-1 and AF-2 domains transcriptional synergistic activity. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specicic manner; the function probbaly involves association with histone deacetylases, such as HDAC1.<ref>PMID:10409727</ref> <ref>PMID:11250900</ref> <ref>PMID:12527917</ref> <ref>PMID:15298701</ref> <ref>PMID:15660129</ref> <ref>PMID:17011493</ref> <ref>PMID:18829551</ref> <ref>PMID:17960593</ref> <ref>PMID:19718048</ref> <ref>PMID:21343338</ref>
[https://www.uniprot.org/uniprot/DDX5_HUMAN DDX5_HUMAN] Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for estrogen receptor ESR1 and androgen receptor AR. Increases ESR1 AF-1 domain-mediated transactivation and ESR1 AF-1 and AF-2 domains transcriptional synergistic activity. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specicic manner; the function probbaly involves association with histone deacetylases, such as HDAC1.<ref>PMID:10409727</ref> <ref>PMID:11250900</ref> <ref>PMID:12527917</ref> <ref>PMID:15298701</ref> <ref>PMID:15660129</ref> <ref>PMID:17011493</ref> <ref>PMID:18829551</ref> <ref>PMID:17960593</ref> <ref>PMID:19718048</ref> <ref>PMID:21343338</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: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: RNA helicase]]
[[Category: Choi YW]]
[[Category: Choi, Y W]]
[[Category: Dutta S]]
[[Category: Dutta, S]]
[[Category: Fielding BC]]
[[Category: Fielding, B C]]
[[Category: Kotaka M]]
[[Category: Kotaka, M]]
[[Category: Tan YJ]]
[[Category: Tan, Y J]]
[[Category: Atp-binding]]
[[Category: Hydrolase]]
[[Category: Rna-binding]]

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