Crystal structure analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis
نویسندگان
چکیده
Yasumitsu Sakamoto1, Saori Roppongi1, Ippei Iizuka1, Yoshio Kusakabe2,3, Tomonobu Umeda2,4, Yuki Odanaka2, Satoko Matsubayashi2, Yasuyuki Kitagawa2,4, Takamasa Nonaka1 and Nobutada Tanaka2,* 1School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan 2School of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan 3Faculty of Pharma Sciences, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan 4Yokohama University of Pharmacy, 601 Matano-cho, Totsuka-ku, Yokohama, Kanagawa 245-0066, Japan
منابع مشابه
Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity
The dipeptidyl peptidase 11 from Porphyromonas gingivalis (PgDPP11) belongs to the S46 family of serine peptidases and preferentially cleaves substrates with Asp/Glu at the P1 position. The molecular mechanism underlying the substrate specificity of PgDPP11, however, is unknown. Here, we report the crystal structure of PgDPP11. The enzyme contains a catalytic domain with a typical double β-barr...
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