Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface

The remarkably efficient suppression of amyloid fibril formation by the DNAJB6 chaperone is dependent on a set of conserved S/T-residues and an oligomeric structure, features unusual among DNAJ chaperones. We explored the structure of DNAJB6 using a combination of structural methods. Lysine-specific...

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Detalles Bibliográficos
Autores principales: Söderberg, Christopher A. G., Månsson, Cecilia, Bernfur, Katja, Rutsdottir, Gudrun, Härmark, Johan, Rajan, Sreekanth, Al-Karadaghi, Salam, Rasmussen, Morten, Höjrup, Peter, Hebert, Hans, Emanuelsson, Cecilia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5979959/
https://www.ncbi.nlm.nih.gov/pubmed/29581438
http://dx.doi.org/10.1038/s41598-018-23035-9

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5979959/
https://www.ncbi.nlm.nih.gov/pubmed/29581438
http://dx.doi.org/10.1038/s41598-018-23035-9

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