Huntingtin and Huntington's Disease

This website was created as a project for Genetics 677 at UW-Madison in the spring of 2009

Thee Dimensional Protein Structure

3D Structure from Swiss-PdbViewer

The following images of amino acid residues 201-327 were taken from the Swiss-PdbViewer program under the entry 2D3X (1). 

Above:  A basic rendering of the three dimensional structure the 201-327 residues of huntingtin.

Above:  A three dimensional surface rendering of the the 201-327 region of the huntingtin protein.

Above:  A structural rendering of huntingtin showing hydrogen bonds within the protein.

Above:  A rendering of the electrostatic  potential of huntingtin in the 201-3


The following image is a another representation of residues 201-327 (model 3D2X) from the PDBSum page (2). 


The three dimensional structures shown here offer some interesting insight into possibly uncovering more information on the molecular function of huntingtin, but is of course very limited by the relatively small amount of amino acids used from the protein sequence.  Here, we only see residues 201-327, out of a total of 3,144.  Of course, there is relevance to studying this section of the protein.  Since huntingtin is cleaved somewhere between residues 400 and 490, this section would hold relative importance in the intranuclear inclusions formed in Huntington's disease.  Studying the structure of these inclusions may be important in figuring out the actual function of the aggregates in inducing apoptosis and neuron death, as seen in Huntington's disease. 


(1)  Scott, DL.  Three-dimensional homology model of huntingtin residues 201- 327.
(2)  Scott, DL.  Three-dimensional homology model of huntingtin residues 201- 327.

Created by Eric Nickels     5/9/2009      Genetics 677 Webpage