| abstract |
PROBLEM TO BE SOLVED: To bind a calcium ion to a three-dimensional structure of PAD4 in the absence of calcium, a mutant (C645A) inactivated by replacing Cys645, which is one of active residues, with Ala, and an active residue Calcium ion and substrate (BA, benzoyl-L-arginine ethylester: BAEE, benzol-glycyl) -L-arginine: BGA, KQTARKSTGG: H3 peptide 1, KAPRKQLATK: H3 peptide 2 and SGRGKGGKGL: H4 peptide) complex structure was determined by X-ray crystal structure analysis, and the structure of both was compared Thus, by analyzing the mechanism of protein deimination by PAD4 and the role of calcium ions, new substances that inhibit protein deimination can be designed and used for the development of new drugs for rheumatoid arthritis. To do. A crystal of peptidylarginine deiminase 4 or a mutant protein thereof belonging to space group C2. Its manufacturing method. A method for searching for a substance capable of binding to peptidylarginine deiminase 4 or a mutant protein thereof. [Selection] Figure 6 |