Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity

Small heat-shock proteins (sHsps) prevent aggregation of thermosensitive client proteins in a first line of defense against cellular stress. The mechanisms by which they perform this function have been hard to define due to limited structural information; currently, there is only one high-resolution...

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Detalles Bibliográficos
Autores principales: Rutsdottir, Gudrun, Härmark, Johan, Weide, Yoran, Hebert, Hans, Rasmussen, Morten I., Wernersson, Sven, Respondek, Michal, Akke, Mikael, Højrup, Peter, Koeck, Philip J. B., Söderberg, Christopher A. G., Emanuelsson, Cecilia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2017
Materias:
Protein Structure and Folding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5427286/
https://www.ncbi.nlm.nih.gov/pubmed/28325834
http://dx.doi.org/10.1074/jbc.M116.766816

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