PA is a 80-kDa subunit and can be cleaved into two
independent domains (10, 11), as follows: a smaller N-terminal
domain with cap-dependent endonuclease activity (6,
23) and a larger C-terminal domain that mediates the interaction
with PB1 (13, 20). The recent crystal structures of the
N-terminal PA domain, termed PAN, confirmed its endonuclease
activity (6, 23), although the mode of substrate binding,
cleavage mechanism, and metal dependence by PAN
remains unclear.
PA is a 80-kDa subunit and can be cleaved into twoindependent domains (10, 11), as follows: a smaller N-terminaldomain with cap-dependent endonuclease activity (6,23) and a larger C-terminal domain that mediates the interactionwith PB1 (13, 20). The recent crystal structures of theN-terminal PA domain, termed PAN, confirmed its endonucleaseactivity (6, 23), although the mode of substrate binding,cleavage mechanism, and metal dependence by PANremains unclear.
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