[HTML][HTML] The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly
R Toso, H Zhu, RM Camire - Journal of biological chemistry, 2008 - ASBMB
Zymogens of the chymotrypsin-like serine protease family are converted to the protease
state following insertion of a newly formed, highly conserved N terminus. This transition is
accompanied by active site formation and ordering of several surface loops in the catalytic
domain. Here we show that disruption of this transition in factor X through mutagenesis (FXa
I16L and FXa V17A) not only alters active site function, but also significantly impairs Na+
and factor Va binding. Active site binding was improved in the presence of high NaCl or with …
state following insertion of a newly formed, highly conserved N terminus. This transition is
accompanied by active site formation and ordering of several surface loops in the catalytic
domain. Here we show that disruption of this transition in factor X through mutagenesis (FXa
I16L and FXa V17A) not only alters active site function, but also significantly impairs Na+
and factor Va binding. Active site binding was improved in the presence of high NaCl or with …
