1LAY

CRYSTAL STRUCTURE OF CYTOMEGALOVIRUS PROTEASE

1LAY の概要

• エントリーDOI: 10.2210/pdb1lay/pdb
• 分子名称: CYTOMEGALOVIRUS PROTEASE (2 entities in total)
• 機能のキーワード: viral protease, serine protease, cytomegalovirus
• 由来する生物種: Cytomegalovirus
• 細胞内の位置: Protease precursor: Host cytoplasm. Assemblin: Host nucleus. Assembly protein: Host nucleus: P16753
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28101.55

構造登録者

Qiu, X.,Culp, J.S.,Dilella, A.G.,Hellmig, B.,Hoog, S.S.,Jason, C.A.,Smith, W.W.,Abdel-Meguid, S.S. (登録日: 1996-07-16, 公開日: 1997-09-26, 最終更新日: 2024-02-14)

主引用文献

Qiu, X.,Culp, J.S.,DiLella, A.G.,Hellmig, B.,Hoog, S.S.,Janson, C.A.,Smith, W.W.,Abdel-Meguid, S.S.
Unique fold and active site in cytomegalovirus protease.
Nature, 383:275-279, 1996

PubMed Abstract: Human herpesviruses are responsible for a variety of diseases. They are divided into three subfamilies: alpha includes herpes simplex viruses (HSV-1 and HSV-2) and varicella-zoster virus (VZV); beta includes cytomegalovirus (CMV) and human herpesvirus-6 (HHV-6); and gamma includes Epstein-Barr virus (EBV). Each virus encodes a serine protease that is essential for its replication and is a potential target for therapeutic intervention. Human CMV is a ubiquitous opportunistic pathogen that can result in life-threatening infections in congenitally infected infants, immunocompromised individuals and immunosuppressed cancer or transplant patients. Here we report the crystal structure of human CMV protease at 2.5 angstroms resolution. The structure reveals a fold that has not been reported for any other serine protease, and an active site consisting of a novel catalytic triad in which the third member is a histidine instead of an aspartic acid, or possibly a catalytic tetrad consisting of a serine, two histidines and an aspartic acid. An unusual dimer interface that is important to the protease activity has also been identified.

PubMed: 8805707
DOI: 10.1038/383275a0

実験手法

X-RAY DIFFRACTION (2.5 Å)