3io4

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[[Image:3io4.png|left|200px]]
 
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{{STRUCTURE_3io4| PDB=3io4 | SCENE= }}
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==Huntingtin amino-terminal region with 17 Gln residues - Crystal C90==
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<StructureSection load='3io4' size='340' side='right'caption='[[3io4]], [[Resolution|resolution]] 3.63&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3io4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IO4 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]] 3.63&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3io4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3io4 OCA], [https://pdbe.org/3io4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3io4 RCSB], [https://www.ebi.ac.uk/pdbsum/3io4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3io4 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/HD_HUMAN HD_HUMAN] Juvenile Huntington disease;Huntington disease. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/HD_HUMAN HD_HUMAN] May play a role in microtubule-mediated transport or vesicle function.[https://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (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/io/3io4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3io4 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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Huntington's disease is a genetic neurodegenerative disorder resulting from polyglutamine (polyQ) expansion (&gt;36Q) within the first exon of Huntingtin (Htt) protein. We applied X-ray crystallography to determine the secondary structure of the first exon (EX1) of Htt17Q. The structure of Htt17Q-EX1 consists of an amino-terminal alpha helix, poly17Q region, and polyproline helix formed by the proline-rich region. The poly17Q region adopts multiple conformations in the structure, including alpha helix, random coil, and extended loop. The conformation of the poly17Q region is influenced by the conformation of neighboring protein regions, demonstrating the importance of the native protein context. We propose that the conformational flexibility of the polyQ region observed in our structure is a common characteristic of many amyloidogenic proteins. We further propose that the pathogenic polyQ expansion in the Htt protein increases the length of the random coil, which promotes aggregation and facilitates abnormal interactions with other proteins in cells.
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===Huntingtin amino-terminal region with 17 Gln residues - Crystal C90===
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Secondary structure of Huntingtin amino-terminal region.,Kim MW, Chelliah Y, Kim SW, Otwinowski Z, Bezprozvanny I Structure. 2009 Sep 9;17(9):1205-12. PMID:19748341<ref>PMID:19748341</ref>
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{{ABSTRACT_PUBMED_19748341}}
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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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==About this Structure==
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<div class="pdbe-citations 3io4" style="background-color:#fffaf0;"></div>
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[[3io4]] is a 3 chain structure of [[Maltose-binding protein]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12,_homo_sapiens Escherichia coli k-12, homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IO4 OCA].
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==See Also==
==See Also==
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*[[Maltose-binding protein|Maltose-binding protein]]
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*[[Huntingtin|Huntingtin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:019748341</ref><references group="xtra"/>
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__TOC__
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[[Category: Escherichia coli k-12, homo sapiens]]
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</StructureSection>
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[[Category: Bezprozvanny, I.]]
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[[Category: Escherichia coli O157:H7]]
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[[Category: Chelliah, Y.]]
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[[Category: Homo sapiens]]
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[[Category: Kim, M W.]]
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[[Category: Large Structures]]
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[[Category: Kim, S W.]]
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[[Category: Bezprozvanny I]]
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[[Category: Otwinowski, Z.]]
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[[Category: Chelliah Y]]
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[[Category: Apoptosis]]
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[[Category: Kim MW]]
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[[Category: Disease mutation]]
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[[Category: Kim SW]]
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[[Category: Hd]]
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[[Category: Otwinowski Z]]
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[[Category: Htt18q-ex1]]
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[[Category: Huntingtin]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Signaling protein]]
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[[Category: Sugar transport]]
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[[Category: Transport]]
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Current revision

Huntingtin amino-terminal region with 17 Gln residues - Crystal C90

PDB ID 3io4

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