4wth
From Proteopedia
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<StructureSection load='4wth' size='340' side='right' caption='[[4wth]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='4wth' size='340' side='right' caption='[[4wth]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4wth]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WTH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wth]] is a 2 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=4WTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WTH FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</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">[[4ys9|4ys9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ys9|4ys9]]</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=4wth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wth OCA], [http://pdbe.org/4wth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wth RCSB], [http://www.ebi.ac.uk/pdbsum/4wth PDBsum]</span></td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATXN3, ATX3, MJD, MJD1, SCA3 ([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=4wth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wth OCA], [http://pdbe.org/4wth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wth RCSB], [http://www.ebi.ac.uk/pdbsum/4wth PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wth ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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). | [[http://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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | An expansion of polyglutamine (polyQ) sequence in ataxin-3 protein causes spinocerebellar ataxia type 3, an inherited neurodegenerative disorder. The crystal structure of the polyQ-containing carboxy-terminal fragment of human ataxin-3 was solved at 2.2-A resolution. The Atxn3 carboxy-terminal fragment including 14 glutamine residues adopts both random coil and alpha-helical conformations in the crystal structure. The polyQ sequence in alpha-helical structure is stabilized by intrahelical hydrogen bonds mediated by glutamine side chains. The intrahelical hydrogen-bond interactions between glutamine side chains along the axis of the polyQ alpha-helix stabilize the secondary structure. Analysis of this structure furthers our understanding of the polyQ-structural characteristics that likely underlie the pathogenesis of polyQ-expansion disorders. | ||
| + | |||
| + | The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.,Zhemkov VA, Kulminskaya AA, Bezprozvanny IB, Kim M FEBS Open Bio. 2016 Feb 18;6(3):168-78. doi: 10.1002/2211-5463.12029. eCollection, 2016 Mar. PMID:27047745<ref>PMID:27047745</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4wth" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Kim, M]] | [[Category: Kim, M]] | ||
[[Category: Zhemkov, V A]] | [[Category: Zhemkov, V A]] | ||
Revision as of 06:13, 18 April 2018
Ataxin-3 Carboxy Terminal Region - Crystal C2 (triclinic)
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