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Discovery of a Novel Aggregation Domain in the Huntingtin Protein: Implications for the Mechanisms of Htt Aggregation and Toxicity
Author(s) -
Wang ZheMing,
Lashuel Hilal A.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201206561
Subject(s) - huntingtin , domain (mathematical analysis) , computer science , computational biology , chemistry , world wide web , biology , biochemistry , gene , mathematics , mathematical analysis , mutant
Aggravating aggregation : An N‐terminal domain that is in close proximity to the polyQ domain in the huntingtin protein, htt105–138, is shown to be highly aggregation prone (see scheme). Potential cross‐talk between this domain and the polyQ region may play a central role in regulating the aggregation and toxicity of Htt‐N‐terminal fragments.