Extended Data Fig. 6: Binding interactions between VKGC and propeptides of VKDPs.
From: Molecular basis of vitamin-K-driven γ-carboxylation at the membrane interface
a, Binding of the VKDP propeptides (Prop) to the α/β and jellyroll domains. b, Polar interactions at the interface between the α/β and jellyroll domains. c, Sequence alignment of propeptides from human VKDPs and VKGC-binding affinities of these propeptides19. PS, protein S. PZ, protein Z. OCN, osteocalcin. MGP, matrix Gla protein. GRP, Gla-rich protein or unique cartilage matrix-associated protein. The MGP propeptide does not contain the recognition motif for furin cleavage and is not removed in mature protein. Uncommon residues in VKDPs at the three key sites are indicated by red letter, with those known to affect propeptide binding in bold. The sequence logo89 above depicts the residue conservation level at each position. n.g., negligible. d, Cellular γ-carboxylation activities of VKGC mutants at the propeptide binding sites I, II and III. FIX-Gla-PC is used as the γ-carboxylation reporter. Data are mean ± s.d. from n = 3 biological replicates.
