دورية أكاديمية
أعرض في EDS

Huntingtin's spherical solenoid structure enables polyglutamine tract-dependent modulation of its structure and function.

التفاصيل البيبلوغرافية
العنوان: Huntingtin's spherical solenoid structure enables polyglutamine tract-dependent modulation of its structure and function.
المؤلفون: Vijayvargia R; Center for Human Genetic Research, Massachusetts General Hospital, Boston, United States.; Department of Neurology, Harvard Medical School, Boston, United States., Epand R; Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Canada., Leitner A; Department of Biology, Institute of Molecular Systems Biology, Eidgenössische Technische Hochschule Zürich, Zurich, Switzerland., Jung TY; Department of Biological Sciences, Cancer Metastasis Control Center, KAIST Institute for the BioCentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.; Department of Biosciences and Nutrition, Karolinska Institute, Solna, Sweden.; School of Technology and Health, KTH Royal Institute of Technology, Novum, Sweden., Shin B; Center for Human Genetic Research, Massachusetts General Hospital, Boston, United States.; Department of Neurology, Harvard Medical School, Boston, United States., Jung R; Center for Human Genetic Research, Massachusetts General Hospital, Boston, United States.; Department of Neurology, Harvard Medical School, Boston, United States., Lloret A; Center for Human Genetic Research, Massachusetts General Hospital, Boston, United States.; Department of Neurology, Harvard Medical School, Boston, United States., Singh Atwal R; Center for Human Genetic Research, Massachusetts General Hospital, Boston, United States.; Department of Neurology, Harvard Medical School, Boston, United States., Lee H; Department of Biological Sciences, Cancer Metastasis Control Center, KAIST Institute for the BioCentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea., Lee JM; Center for Human Genetic Research, Massachusetts General Hospital, Boston, United States.; Department of Neurology, Harvard Medical School, Boston, United States., Aebersold R; Department of Biology, Institute of Molecular Systems Biology, Eidgenössische Technische Hochschule Zürich, Zurich, Switzerland.; Faculty of Science, University of Zurich, Zurich, Switzerland., Hebert H; Department of Biosciences and Nutrition, Karolinska Institute, Solna, Sweden.; School of Technology and Health, KTH Royal Institute of Technology, Novum, Sweden., Song JJ; Department of Biological Sciences, Cancer Metastasis Control Center, KAIST Institute for the BioCentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea., Seong IS; Center for Human Genetic Research, Massachusetts General Hospital, Boston, United States.; Department of Neurology, Harvard Medical School, Boston, United States.
المصدر: ELife [Elife] 2016 Mar 22; Vol. 5, pp. e11184. Date of Electronic Publication: 2016 Mar 22.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Huntingtin Protein/*chemistry , Huntingtin Protein/*metabolism , Peptides/*metabolism, Biophysical Phenomena ; Circular Dichroism ; Mass Spectrometry ; Microscopy, Electron ; Protein Conformation
مستخلص: The polyglutamine expansion in huntingtin protein causes Huntington's disease. Here, we investigated structural and biochemical properties of huntingtin and the effect of the polyglutamine expansion using various biophysical experiments including circular dichroism, single-particle electron microscopy and cross-linking mass spectrometry. Huntingtin is likely composed of five distinct domains and adopts a spherical α-helical solenoid where the amino-terminal and carboxyl-terminal regions fold to contain a circumscribed central cavity. Interestingly, we showed that the polyglutamine expansion increases α-helical properties of huntingtin and affects the intramolecular interactions among the domains. Our work delineates the structural characteristics of full-length huntingtin, which are affected by the polyglutamine expansion, and provides an elegant solution to the apparent conundrum of how the extreme amino-terminal polyglutamine tract confers a novel property on huntingtin, causing the disease.
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معلومات مُعتمدة: 233226 International ERC_ European Research Council; R01 NS079651 United States NS NINDS NIH HHS
فهرسة مساهمة: Keywords: HEAT/HEAT-like repeat; Huntington's disease; biophysics; neurodegenerative disorders; neuroscience; none; solenoid scaffold protein; structural biology
المشرفين على المادة: 0 (HTT protein, human)
0 (Huntingtin Protein)
0 (Peptides)
26700-71-0 (polyglutamine)
تواريخ الأحداث: Date Created: 20160323 Date Completed: 20161213 Latest Revision: 20220129
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC4846397
DOI: 10.7554/eLife.11184
PMID: 27003594
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.11184