Topographical relationships between the monovalent and divalent cation binding sites of des-1-41-light chain bovine plasma protein C and des-1-41-light chain-activated bovine plasma protein C.

K A Hill, F J Castellino

Index: J. Biol. Chem. 262(15) , 7105-8, (1987)

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Abstract

The paramagnetic effect of Mn2+ on the longitudinal relaxation rate (T1)-1 of 205Tl+, when both cations are bound to des-1-41-light chain bovine plasma protein C (GDPC) and its activation product, des-1-41-light chain-activated bovine plasma protein C (GDAPC), has been assessed by 205Tl+ NMR spectroscopy. A substantial shortening of the T1 for Tl+ bound to either protein was observed in the presence of Mn2+, an effect not noted upon substitution of Mn2+ with the diamagnetic cation Ca2+, which is known to bind to these proteins in a similar fashion to Mn2+. This paramagnetic effect was employed to estimate distances between the monovalent and divalent cation sites in these proteins, approximately 6.7 +/- 0.2 A with GDPC and 8.3 +/- 0.2 A in GDAPC. These data suggest that a conformational alteration occurs upon activation of GDPC which leads to an increase in the distance between the monovalent and divalent cation sites.