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- W1554627437 abstract "Anticoagulant protein S interacts with the complement regulatory protein C4b‐binding protein (C4BP) via its sex‐hormone‐binding globulin (SHB6)‐like region, which contains two globular (G) domains. Similar G domains are found in Gas6, a protein homologous to protein S, which is not known to bind C4BP or to have any anticoagulant activity. To determine the relative importance of the two G domains in protein S for C4BP protein binding, three recombinant protein S chimeras were produced having either of the two globular domains, or the whole SHB6‐like globulin region, replaced by corresponding parts from Gas6. The chimeras were tested for binding to immobilized C4BP using surface‐plasmon‐resonance technology and microtiter plate‐based assays. In both systems, chimeras containing either only globular domains G1 or G2 from protein S were found to bind C4BP. Binding was stimulated by Ca 2+ in a manner similar to that found for wild‐type protein S. The affinities for C4BP of both chimeras containing individual G domains from protein S, were lower than that of wild‐type protein S. Chimera II, containing the G1 domain from protein S, consistently bound C4BP more efficiently than chimera I, which had the protein S‐derived G2 domain. The chimera containing the whole SHB6‐like globulin region from Gas6 interacted considerably more weakly with C4BP. Our results demonstrate that both G domains of protein S are involved in the interaction between protein S and C4BP and that full affinity binding is dependent on contributions from both domains." @default.
- W1554627437 created "2016-06-24" @default.
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- W1554627437 date "1999-12-15" @default.
- W1554627437 modified "2023-10-17" @default.
- W1554627437 title "Both G-type domains of protein S are required for the high-affinity interaction with C4b-binding protein" @default.
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- W1554627437 doi "https://doi.org/10.1046/j.1432-1327.1999.00928.x" @default.
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