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APC — ARG1

Text-mined interactions from Literome

Yegneswaran et al., J Biol Chem 2007 : The peptide inhibited the APC dependent cleavage of both Arg ( 506 ) and Arg ( 306 ) because inhibition was observed with plasma derived fVa and recombinant R506Q and RR306/679QQ fVa
Balusu et al., Biochemistry 2007 : In this study, we have mapped the APC interaction site in Pol-beta and have found that Thr79, Lys81, and Arg83 of Pol-beta were critical for its interaction with APC
Andersson et al., Blood 2010 : In a purified assay using FVa R506Q/R679Q, purified protein S D95A was shown to have greatly reduced ability to enhance APC induced cleavage of FVa Arg306
Nicolaes et al., J Biol Chem 2010 : APC ( S360A ) binding to FVa was critically dependent upon the presence of Arg ( 506 ) and not Arg ( 306 ) and additionally required an active site accessible to substrates ... Our results show that despite exosite interactions near the Arg ( 506 ) cleavage site, binding of APC ( S360A ) to FVa is almost completely dependent on Arg ( 506 ) interacting with APC ( S360A ) to form a nonproductive Michaelis complex