@article{oai:jaxa.repo.nii.ac.jp:00022656,
 author = {阪本, 泰光 and 鈴木, 義之 and 飯塚, 一平 and 館岡, 千佳 and 六本木, 沙織 and 藤本, 真友 and 伊中, 浩治 and 田仲, 広明 and 山田, 貢 and 太田, 和敬 and 合田, 浩明 and 野中, 孝昌 and 小笠原, 渉 and 田中, 信忠 and Sakamoto, Yasumitsu and Suzuki, Yoshiyuki and Iizuka, Ippei and Tateoka, Chika and Roppongi, Saori and Fujimoto, Mayu and Inaka, Koji and Tanaka, Hiroaki and Yamada, Mitsugu and Ohta, Kazunori and Gouda, Hiroaki and Nonaka, Takamasa and Ogasawara, Wataru and Tanaka, Nobutada},
 journal = {Scientific Reports},
 month = {Jun},
 note = {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-barrel fold and a recently identified regulatory α-helical domain. Crystal structure analyses, docking studies, and biochemical studies revealed that the side chain of Arg673 in the S1 subsite is essential for recognition of the Asp/Glu side chain at the P1 position of the bound substrate. Because S46 peptidases are not found in mammals and the Arg673 is conserved among DPP11s, we anticipate that DPP11s could be utilised as targets for antibiotics. In addition, the present structure analyses could be useful templates for the design of specific inhibitors of DPP11s from pathogenic organisms., 形態: カラー図版あり, Physical characteristics: Original contains color illustrations, 資料番号: PA1610029000},
 title = {Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity},
 volume = {5},
 year = {2015}
}