Extended Data Fig. 4: Sequence alignment of human Gla proteins and the structures of Gla domains.
From: Structure and mechanism of vitamin-K-dependent γ-glutamyl carboxylase
a, Sequence alignment of the propeptide and Gla domain of human Prothrombin (Factor II, F2), Factor VII (F7), Factor IX (F9), Factor X (F10), Protein C, Protein S, Protein Z, Transmembrane Gla proteins (TMGs) 1-4, Growth arrest-specific gene 6 (Gas6), Matrix Gla protein (MGP) and BGP. The propeptide and Gla domain are indicated by brown and orange lines, respectively. The conserved -16, -10 and -6 positions of the propeptide are labeled above the sequence. The disulfide bonds in Gla domains are indicated by black lines. The residues of BGP observed in the GGCX–BGP structure are indicated by a red rectangle. b and c, Crystal structures of the mature Gla domain of human F9 (PDB: 1NL0, light orange) (b) and mature porcine BGP (PDB: 1Q8H, grey) (c). The side chains of Gla residues are shown as sticks and Ca2+ ions are shown as green balls. d, Cryo-EM structure of unmature human BGP in GGCX–BGP complex. The propeptide and Gla domain are shown in brown and orange, respectively. The invisible residues are indicated by dashed lines.
