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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 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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| 言語種別 | 英語 |
| 発行・発表の年月 | 1996/09 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad |
| 執筆形態 | その他 |
| 掲載誌名 | CELL |
| 出版社・発行元 | CELL PRESS |
| 巻・号・頁 | 86(5),pp.835-843 |
| 著者・共著者 | P Chen,H Tsuge,RJ Almassy,CL Gribskov,S Katoh,DL Vanderpool,SA Margosiak,C Pinko,DA Matthews,CC Kan |
| 概要 | Proteolytic processing of capsid assembly protein precursors by herpesvirus proteases is essential for virion maturation. A 2.5 Angstrom crystal structure of the human cytomegalovirus protease catalytic domain has been determined by X-ray diffraction. The structure defines a new class of serine protease with respect to global-fold topology and has a catalytic triad consisting of Ser-132, His-63, and His-157 in contrast with the Ser-His-Asp triads found in other serine proteases. However, catalytic machinery for activating the serine nucleophile and stabilizing a tetrahedral transition state is oriented similarly to that for members of the trypsin-like and subtilisin-like serine protease families. Formation of the active dimer is mediated primarily by burying a helix of one protomer into a deep cleft in the protein surface of the other. |
| DOI | 10.1016/S0092-8674(00)80157-9 |
| ISSN | 0092-8674 |