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PLoS Computational Biology Issue Image | Vol. 5(3) March 2009

PLoS Computational Biology Issue Image | Vol. 5(3) March 2009

PLOS
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Nearing the structure of the human huntingtin protein.

For many years, it has been known that mutations in the human huntingtin protein are responsible for Huntington chorea, a neurodegenerative disease. However, very little is known about the structure and function of this long protein. Using a computational method on a sequence alignment of huntingtin with its orthologs (output shown in the background), we have predicted that this protein contains three elongated domains (alpha-rods, yellow cylinders) that are involved in intramolecular (left) and intermolecular (right) interactions (see Palidwor et al., doi:10.1371/journal.pcbi.1000304). This work opens avenues for further characterization of huntingtin and other proteins with alpha-rods.

Image Credit: Cartoon created using Google SketchUp and BiasViz by Miguel Andrade-Navarro (Max Delbrück Center for Molecular Medicine, Germany).

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Nearing the structure of the human huntingtin protein.

For many years, it has been known that mutations in the human huntingtin protein are responsible for Huntington chorea, a neurodegenerative disease. However, very little is known about the structure and function of this long protein. Using a computational method on a sequence alignment of huntingtin with its orthologs (output shown in the background), we have predicted that this protein contains three elongated domains (alpha-rods, yellow cylinders) that are involved in intramolecular (left) and intermolecular (right) interactions (see Palidwor et al., doi:10.1371/journal.pcbi.1000304). This work opens avenues for further characterization of huntingtin and other proteins with alpha-rods.

Image Credit: Cartoon created using Google SketchUp and BiasViz by Miguel Andrade-Navarro (Max Delbrück Center for Molecular Medicine, Germany).

https://doi.org/10.1371/image.pcbi.v05.i03.g001