Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

Article Abstract:

A study was conducted to determine the crystal structure of thermosome, the archeal group II chaperonin frm Thermoplasma acidophilum and homolog of the eucharyotic chaperonin CCT/TRiC. Data shows that domain folds in the CCT/TRiC subunit assembly are homologous to group I chaperonins that occur in eubacteria but form a type of inter-ring contact. Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the adenosine triphosphate-stabilized form.

Author: Huber, Robert, Lowe, Jan, Huber, Harald, Ditzel, Lars, Stock, Daniela, Stetter, Karl-Otto, Steinbacher, Stefan
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
Research, Proteins, Archaeabacteria, Protein conformation, Archaea, Protista, Protists

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Prion protein biology

Article Abstract:

Neurodegenerative diseases such as the Creutzfeldt-Jakob disease, bovine spongiform encephalopathy and scrapie are known to have been caused by the aberrant metabolism and resulting accumulation of the prion protein (Prp). Previous studies have revealed the genetic and infectious origins of these diseases. This resulted to the discovery of 20 different mutations in the human Prp gene.

Author: Prusiner, Stanley B., DeArmond, Stephen J., Cohen, Fred E., Scott, Michael R.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
Genetic aspects, Nervous system, Prions, Prions (Proteins), Nerve degeneration

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