Article
Conserved L464 in p97 D1-D2 linker is critical for p97 cofactor regulated ATPase activity.
The Biochemical journal - 17 Sept 2021
Zhang Xiaoyi, Gui Lin, Li Shan, Nandi Purbasha, Columbres Rod Carlo, Wong Daniel E, Moen Derek R, Lin Henry J, Chiu Po-Lin, Chou Tsui-Fen
Abstract excerpt
p97 protein is a highly conserved, abundant, functionally diverse, structurally dynamic homohexameric AAA enzyme-containing N, D1, and D2 domains. A truncated p97 protein containing the N and D1 domains and the D1-D2 linker (ND1L) exhibits 79% of wild-type (WT) ATPase activity whereas the ND1 domain alone without the linker only has 2% of WT activity. To investigate the relationship between the D1-D2 linker and...
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