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

• Main Authors: 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
• 其他作者: School of Biological Sciences
• 格式: Article
• 語言: English
• 出版: 2018
• 主題: Chaperones; Small-angle X-ray Scattering (SAXS)
• 在線閱讀: https://hdl.handle.net/10356/87375; http://hdl.handle.net/10220/45394

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...