GroEL: More than Just a folding cage.
The chaperonin GroEL has been thought of as an important but passive player in protein folding, providing an encapsulated environment that allows folding to proceed unimpaired by aggregation. In this issue, Tang et al. (2006) redesign the GroEL central cavity and show that the chaperonin cage can alter the rate of folding and, for some proteins, could even alter the folding mechanism.
Radford
Sheena E
SE
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom. s.e.radford@leeds.ac.uk
D020816:Amino Acid Motifs / Q000502:physiology; D000595:Amino Acid Sequence / Q000502:physiology; D001419:Bacteria / Q000737:chemistry / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008970:Molecular Weight; D011487:Protein Conformation; D017510:Protein Folding
D018834:Chaperonin 60