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Molecular chaperones: structure of a protein disaggregase
Authors:Mogk Axel  Bukau Bernd
Affiliation:1ZMBH, Universit?t Heidelberg, Im Neuenheimer Feld 282, D-69120, Heidelberg, Germany. a.mogk@zmbh.uni-heidelberg.de
Abstract:The ring-forming molecular chaperone Hsp104/ClpB is a member of the AAA+ protein family which rescues proteins from aggregated states. The newly determined crystal structure of ClpB provides new insights into the mechanism of protein disaggregation, suggesting a crowbar activity mediated by a unique coiled-coil domain.
Keywords:
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