蛋白質におけるアスパラギン酸の異性化 Isomerization of Aspartic Acid in Protein
Aspartic acid in protein isomerizes autocatalytically to isoaspartate <I>via</I> succinimide intermediate <I>in vitro</I> and <I>in vivo</I>. We have determined the crystal structures of <I>Ustilago sphaerogena</I> ribonuclease U<SUB>2</SUB> with an isoaspartate residue and hen egg-white lysozymes with a succinimide intermediate and with an isoaspartate residue at 1.8 Å resolution. These crystal structures reveal that the isomerizations of aspartic acids induce structural changes on proteins, which result in modifying the function and physical properties of the proteins.
日本結晶学会誌 40(4), 272-278, 1998-08-28
The Crystallographic Society of Japan