3ior

<StructureSection load='3ior' size='340' side='right' caption='[[3ior]], [[Resolution|resolution]] 3.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ior]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IOR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3io4|3io4]], [[3io6|3io6]], [[3iot|3iot]], [[3iou|3iou]], [[3iov|3iov]], [[3iow|3iow]]</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=3ior FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ior OCA], [http://pdbe.org/3ior PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ior RCSB], [http://www.ebi.ac.uk/pdbsum/3ior PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ior ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/io/3ior_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3ior" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Kim, M W]]

[[Category: Htt-ex1]]

[[Category: Huntingtin]]

[[Category: Nucleus]]

[[Category: Phosphoprotein]]

[[Category: Transport]]