Structural highlights
4ys9 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 4wth |
| Gene: | ATXN3, ATX3, MJD, MJD1, SCA3 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhemkov VA, Kulminskaya AA, Bezprozvanny IB, Kim M. The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3. FEBS Open Bio. 2016 Feb 18;6(3):168-78. doi: 10.1002/2211-5463.12029. eCollection, 2016 Mar. PMID:27047745 doi:http://dx.doi.org/10.1002/2211-5463.12029
