1ib2

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(New page: 200px<br /> <applet load="1ib2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ib2, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1ib2.gif|left|200px]]<br />
 
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<applet load="1ib2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ib2, resolution 1.90&Aring;" />
 
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'''CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN==
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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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<StructureSection load='1ib2' size='340' side='right'caption='[[1ib2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== 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/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='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='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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<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>
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</table>
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== 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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/1ib2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<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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==About this Structure==
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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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1IB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IB2 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11336708 11336708]
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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/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[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: BME]]
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[[Category: puf motif]]
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[[Category: pumilio-homology domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:28:26 2007''
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CRYSTAL STRUCTURE OF A PUMILIO-HOMOLOGY DOMAIN

PDB ID 1ib2

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