4WTH

Ataxin-3 Carboxy Terminal Region - Crystal C2 (triclinic)

Summary for 4WTH

• Entry DOI: 10.2210/pdb4wth/pdb
• Related: 4YS9
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein, Ataxin-3 chimera, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ZINC ION, ... (4 entities in total)
• Functional Keywords: ataxin-3, polyglutamine helix, nerve tissue proteins, polyq, triplet repeat disorder, transcription
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 98229.92

Authors

Zhemkov, V.A.,Kim, M. (deposition date: 2014-10-30, release date: 2016-03-09, Last modification date: 2023-09-27)

Primary citation

Zhemkov, V.A.,Kulminskaya, A.A.,Bezprozvanny, I.B.,Kim, M.
The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.
FEBS Open Bio, 6:168-178, 2016

PubMed Abstract: 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-Å resolution. The Atxn3 carboxy-terminal fragment including 14 glutamine residues adopts both random coil and α-helical conformations in the crystal structure. The polyQ sequence in α-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 α-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.

PubMed: 27047745
DOI: 10.1002/2211-5463.12029

Experimental method

X-RAY DIFFRACTION (2.25 Å)