This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4ys9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 11: Line 11:
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4ys9" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
Line 17: Line 28:
[[Category: Zhemkov, V A]]
[[Category: Zhemkov, V A]]
[[Category: Ataxia]]
[[Category: Ataxia]]
-
[[Category: Ataxin-3]]
 
[[Category: Ataxin]]
[[Category: Ataxin]]
 +
[[Category: Ataxin-3]]
[[Category: Huntington's disease]]
[[Category: Huntington's disease]]
[[Category: Polyglutamine]]
[[Category: Polyglutamine]]
[[Category: Transcription]]
[[Category: Transcription]]
[[Category: Triplet repeat disorder]]
[[Category: Triplet repeat disorder]]

Revision as of 06:16, 18 April 2018

Ataxin-3 Carboxy-Terminal Region - Crystal C1 (tetragonal)

4ys9, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools