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カトウ ケイコ
KATO KEIKO
加藤 啓子 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 期間 | 1999/02 |
| 名称 | Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis |
| 区分 | その他 |
| 開催場所 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC JOURNAL OF BIOLOGICAL CHEMISTRY |
| 発表者・共同発表者等 | A Kishi,M Kato,T Shimizu,K Kato,K Matsumoto,S Yoshida,S Shiosaka,T Hakoshima |
| 発表・展示等 | Neuropsin is a novel serine protease, the expression of which is highly localized in the limbic areas of the mouse brain and which is suggested to be involved in kindling epileptogenesis and hippocampal plasticity, The 2.1-Angstrom resolution crystal structure of neuropsin provides the first three-dimensional view of one of the serine proteases highly expressed in the nervous system, and reveals a serine protease fold that exhibits chimeric features between trypsin and nerve growth factor-gamma (NGF gamma), a member of the kallikrein family. Neuropsin possesses an N-glycosylated "kallikrein loop" but forms six disulfide bonds corresponding to those of trypsin, The ordered kallikrein loop projects proline toward the active site tee restrict smaller residues or proline at the P2 position of substrates. Loop F, which participates in forming the S3/S4 sites, is similar to trypsin rather than NGF gamma. The unique conformations of loops G and H form an S1 pocket specific for both arginine and lysine, These characteristic loop structures forming the substrate-binding site suggest the novel substrate specificity of neuropsin and give a clue to the design of its specific inhibitors. |
| DOI | 10.1074/jbc.274.7.4220 |