Literature summary for 3.4.22.60 extracted from

Riedl, S.J.; Fuentes-Prior, P.; Renatus, M.; Kairies, N.; Krapp, S.; Huber, R.; Salvesen, G.S.; Bode, W.
Structural basis for the activation of human procaspase-7 (2001), Proc. Natl. Acad. Sci. USA, 98, 14790-14795.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
2.9 A crystal structure of recombinant C285A procaspase, sitting drop vapor diffusion method	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C285A	mutant procaspase-7 shows no autoactivation	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
35000	-	2 * 35000, procaspase-7 C285A mutant, in the homodimeric procaspase-7 each monomer is organized in two structured subdomains connected by partially flexible linkers, which asymmetrically occupy and block the central cavity, SDS-PAGE	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P55210	-	-

Subunits

Subunits	Comment	Organism
More	2 * 35000, procaspase-7 C285A mutant, in the homodimeric procaspase-7 each monomer is organized in two structured subdomains connected by partially flexible linkers, which asymmetrically occupy and block the central cavity, SDS-PAGE	Homo sapiens

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Release 2023.1 (January 2023)