1ib2

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<StructureSection load='1ib2' size='340' side='right'caption='[[1ib2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1ib2' size='340' side='right'caption='[[1ib2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ib2]] 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=1IB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IB2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ib2]] 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=1IB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IB2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ib3|1ib3]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></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=1ib2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ib2 OCA], [https://pdbe.org/1ib2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ib2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ib2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ib2 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=1ib2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ib2 OCA], [https://pdbe.org/1ib2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ib2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ib2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ib2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PUM1_HUMAN PUM1_HUMAN]] Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity).
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[https://www.uniprot.org/uniprot/PUM1_HUMAN PUM1_HUMAN] Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ib2 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ib2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Puf proteins regulate translation and mRNA stability by binding sequences in their target RNAs through the Pumilio homology domain (PUM-HD), which is characterized by eight tandem copies of a 36 amino acid motif, the PUM repeat. We have solved the structure of the PUM-HD from human Pumilio1 at 1.9 A resolution. The structure reveals that the eight PUM repeats correspond to eight copies of a single, repeated structural motif. The PUM repeats pack together to form a right-handed superhelix that approximates a half doughnut. The distribution of side chains on the inner and outer faces of this half doughnut suggests that the inner face of the PUM-HD binds RNA while the outer face interacts with proteins such as Nanos, Brain Tumor, and cytoplasmic polyadenylation element binding protein.
 
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Crystal structure of a Pumilio homology domain.,Wang X, Zamore PD, Hall TM Mol Cell. 2001 Apr;7(4):855-65. PMID:11336708<ref>PMID:11336708</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1ib2" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hall, T M.T]]
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[[Category: Hall TMT]]
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[[Category: Wang, X]]
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[[Category: Wang X]]
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[[Category: Zamore, P D]]
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[[Category: Zamore PD]]
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[[Category: Puf motif]]
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[[Category: Pumilio-homology domain]]
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[[Category: Rna binding protein]]
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Revision as of 07:45, 3 April 2024

CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN

PDB ID 1ib2

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