Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.
Newly solved chaperone structures include the thermosome, a group II chaperonin, and a small heat-shock protein. Novel ideas on chaperone mechanism are presented in the forced unfolding hypothesis of GroEL action. Structures of chaperone-pilin complexes reveal the mechanism of chaperone interaction in bacterial pilus assembly and there have been major advances in understanding the structure and function of Hsp100 unfoldases.
Saibil
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Department of Crystallography, Birkbeck College, London, WC1E 7HX, UK. H.Saibil@mail.cryst.bbk.ac.uk
D000244:Adenosine Diphosphate / Q000502:physiology; D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000145:classification / Q000502:physiology; D000494:Allosteric Regulation; D018835:Chaperonin 10 / Q000737:chemistry / Q000502:physiology; D018834:Chaperonin 60 / Q000737:chemistry / Q000502:physiology; D049071:Endopeptidase Clp; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology; D007136:Immunoglobulins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012697:Serine Endopeptidases / Q000737:chemistry; D013329:Structure-Activity Relationship
D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D007136:Immunoglobulins; D018832:Molecular Chaperones; D000244:Adenosine Diphosphate; D012697:Serine Endopeptidases; D049071:Endopeptidase Clp; D000251:Adenosine Triphosphatases