Nature Communications (May 2019)
Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor
- Albert Escobedo,
- Busra Topal,
- Micha B. A. Kunze,
- Juan Aranda,
- Giulio Chiesa,
- Daniele Mungianu,
- Ganeko Bernardo-Seisdedos,
- Bahareh Eftekharzadeh,
- Margarida Gairí,
- Roberta Pierattelli,
- Isabella C. Felli,
- Tammo Diercks,
- Oscar Millet,
- Jesús García,
- Modesto Orozco,
- Ramon Crehuet,
- Kresten Lindorff-Larsen,
- Xavier Salvatella
Affiliations
- Albert Escobedo
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- Busra Topal
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- Micha B. A. Kunze
- Structural Biology and NMR Laboratory, Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen
- Juan Aranda
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- Giulio Chiesa
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- Daniele Mungianu
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- Ganeko Bernardo-Seisdedos
- CIC bioGUNE
- Bahareh Eftekharzadeh
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- Margarida Gairí
- NMR Facility, Scientific and Technological Centers University of Barcelona (CCiTUB)
- Roberta Pierattelli
- CERM and Department of Chemistry “Ugo Schiff”, University of Florence
- Isabella C. Felli
- CERM and Department of Chemistry “Ugo Schiff”, University of Florence
- Tammo Diercks
- CIC bioGUNE
- Oscar Millet
- CIC bioGUNE
- Jesús García
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- Modesto Orozco
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- Ramon Crehuet
- Institute for Advanced Chemistry of Catalonia (IQAC-CSIC)
- Kresten Lindorff-Larsen
- Structural Biology and NMR Laboratory, Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen
- Xavier Salvatella
- Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology
- DOI
- https://doi.org/10.1038/s41467-019-09923-2
- Journal volume & issue
-
Vol. 10,
no. 1
pp. 1 – 11
Abstract
Polyglutamine (polyQ) tracts are low-complexity regions and their expansion is linked to certain neurodegenerative diseases. Here the authors combine experimental and computational approaches to find that the length of the androgen receptor polyQ tract correlates with its helicity and show that the polyQ helical structure is stabilized by hydrogen bonds between the Gln side chains and main chain carbonyl groups.
