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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Main Authors: | , , , , , , , , , , |
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Other Authors: | |
Format: | Article |
Language: | English |
Published: |
2018
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Subjects: | |
Online Access: | https://hdl.handle.net/10356/87375 http://hdl.handle.net/10220/45394 |
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Institution: | Nanyang Technological University |
Language: | English |
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