Literature summary for 2.7.2.3 extracted from

Osvath, S.; Jackel, M.; Agocs, G.; Zavodszky, P.; Kohler, G.; Fidy, J.
Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase (2006), Proteins Struct. Funct. Bioinform., 62, 909-917.

Search for more literature for 2.7.2.3

Application

Application	Comment	Organism
additional information	submolecular mechanism of amyloid formation based on a model system of PGK, evaluated by microscopic measurements and tryptophan fluorescence. Interactions between the polypeptide chains of the two domains of the protein direct the misfolding process from the early steps to the amyloid formation, and influence the final structure. Kinetics of misfolding is different for the individual domains. Misfolding of the domains within the complete protein is synchronized indicating that domain-domain interactions direct the misfolding and amyloid formation mechanism	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
additional information	mutants HisN W122, HisC W333, His-PGK W122, and His-PGK W333, single tryptophan mutants of the individual N and C terminal domains and the complete protein, amyloid fibrils grow from all mutants under identical conditions as for the wild-type protein	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Saccharomyces cerevisiae

Storage Stability

Storage Stability	Organism
-80°C, 50 mM phosphate buffer, pH 6.2	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
PGK	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)