FIGURE 1.

Schematic presentation of the locations of mutations R594H, G597V, and T604I reported in Bruck syndrome 2 relative to the catalytically critical residues in the C-terminal part of the processed LH2(long) polypeptide. His⁶⁶², Asp⁶⁶⁴, and His⁷¹⁴ correspond to the conserved residues known to be critical for binding of the Fe²⁺ atom in LH1 and several other 2-oxoglutarate-dependent dioxygenases, and Arg⁷²⁴ corresponds to the conserved basic residue required for the binding of the C-5 carboxyl group of 2-oxoglutarate. LH2(long) is a 758-amino acid polypeptide; processed LH2(long) consists of 733 amino acids after cleavage of the 25-residue signal peptide. The amino acids of LH2(long) are numbered according to the processed polypeptide.