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| | <StructureSection load='4wzw' size='340' side='right'caption='[[4wzw]], [[Resolution|resolution]] 2.95Å' scene=''> | | <StructureSection load='4wzw' size='340' side='right'caption='[[4wzw]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wzw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wzw]] is a 3 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wzr|4wzr]]</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=4wzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzw OCA], [https://pdbe.org/4wzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wzw RCSB], [https://www.ebi.ac.uk/pdbsum/4wzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzw ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA0020, XTP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4wzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzw OCA], [http://pdbe.org/4wzw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wzw RCSB], [http://www.ebi.ac.uk/pdbsum/4wzw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PUM3_HUMAN PUM3_HUMAN] Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (PubMed:21266351). Binds to double-stranded RNA or DNA without sequence specificity (PubMed:25512524). Involved in development of the eye and of primordial germ cells (By similarity).[UniProtKB:X1WGX5]<ref>PMID:21266351</ref> <ref>PMID:25512524</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hall, T M.T]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Qiu, C]] | + | [[Category: Hall TMT]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Qiu C]] |
| - | [[Category: Pumilio repeat protein]]
| + | |
| - | [[Category: Rna binding protein-dna complex]]
| + | |
| Structural highlights
Function
PUM3_HUMAN Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (PubMed:21266351). Binds to double-stranded RNA or DNA without sequence specificity (PubMed:25512524). Involved in development of the eye and of primordial germ cells (By similarity).[UniProtKB:X1WGX5][1] [2]
Publication Abstract from PubMed
Pumilio/feminization of XX and XO animals (fem)-3 mRNA-binding factor (PUF) proteins bind sequence specifically to mRNA targets using a single-stranded RNA-binding domain comprising eight Pumilio (PUM) repeats. PUM repeats have now been identified in proteins that function in pre-rRNA processing, including human Puf-A and yeast Puf6. This is a role not previously ascribed to PUF proteins. Here we present crystal structures of human Puf-A that reveal a class of nucleic acid-binding proteins with 11 PUM repeats arranged in an "L"-like shape. In contrast to classical PUF proteins, Puf-A forms sequence-independent interactions with DNA or RNA, mediated by conserved basic residues. We demonstrate that equivalent basic residues in yeast Puf6 are important for RNA binding, pre-rRNA processing, and mRNA localization. Thus, PUM repeats can be assembled into alternative folds that bind to structured nucleic acids in addition to forming canonical eight-repeat crescent-shaped RNA-binding domains found in classical PUF proteins.
A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization.,Qiu C, McCann KL, Wine RN, Baserga SJ, Hall TM Proc Natl Acad Sci U S A. 2014 Dec 15. pii: 201407634. PMID:25512524[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chang HY, Fan CC, Chu PC, Hong BE, Lee HJ, Chang MS. hPuf-A/KIAA0020 modulates PARP-1 cleavage upon genotoxic stress. Cancer Res. 2011 Feb 1;71(3):1126-34. PMID:21266351 doi:10.1158/0008-5472.CAN-10-1831
- ↑ Qiu C, McCann KL, Wine RN, Baserga SJ, Hall TM. A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization. Proc Natl Acad Sci U S A. 2014 Dec 15. pii: 201407634. PMID:25512524 doi:http://dx.doi.org/10.1073/pnas.1407634112
- ↑ Qiu C, McCann KL, Wine RN, Baserga SJ, Hall TM. A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization. Proc Natl Acad Sci U S A. 2014 Dec 15. pii: 201407634. PMID:25512524 doi:http://dx.doi.org/10.1073/pnas.1407634112
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