@article{oai:jaxa.repo.nii.ac.jp:00022705,
 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 正木, 美佳 and 太田, 和敬 and 岡田, 宏文 and 野中, 孝昌 and 森川, 康 and 中村, 和郎 T. 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 Masaki, Mika and Ohta, Kazunori and Okada, Hirofumi and Nonaka, Takamasa and Morikawa, Yasushi and Nakamura, Kazuo  T. and Ogasawara, Wataru and Tanaka, Nobutada},
 journal = {Scientific Reports},
 month = {May},
 note = {The dipeptidyl aminopeptidase BII (DAP BII) belongs to a serine peptidase family, S46. The amino acid sequence of the catalytic unit of DAP BII exhibits significant similarity to those of clan PA endopeptidases, such as chymotrypsin. However, the molecular mechanism of the exopeptidase activity of family S46 peptidase is unknown. Here, we report crystal structures of DAP BII. DAP BII contains a peptidase domain including a typical double b-barrel fold and previously unreported a-helical domain. The structures of peptide complexes revealed that the a-helical domain covers the active-site cleft and the side chain of Asn330 in the domain forms hydrogen bonds with the N-terminus of the bound peptide. These observations indicate that the a-helical domain regulates the exopeptidase activity of DAP BII. Because S46 peptidases are not found in mammals, we expect that our study will be useful for the design of specific inhibitors of S46 peptidases from pathogens., 形態: カラー図版あり, Physical characteristics: Original contains color illustrations, 資料番号: PA1610095000},
 title = {S46 Peptidases are the First Exopeptidases to be Members of Clan PA},
 volume = {4},
 year = {2014}
}