Protein folding is often mediated by molecular chaperones. Recently, a novel class of
intramolecular chaperones has been identified in tailspike proteins of evolutionarily distant
viruses, which require a C-terminal chaperone for correct folding. The highly homologous
chaperone domains are interchangeable between pre-proteins and release themselves
after protein folding. Here we report the crystal structures of two intramolecular chaperone
domains in either the released or the pre-cleaved form, revealing the role of the chaperone�…

Structure of an intramolecular chaperone mediating triple-β-helix folding - NASA/ADS … Structure
of an intramolecular chaperone mediating triple-β-helix folding … Pub Date: August 2010 …