1FL1

KSHV PROTEASE

1FL1 の概要

• エントリーDOI: 10.2210/pdb1fl1/pdb
• 関連するPDBエントリー: 1AT3 1CMV 1LAY 1VZV 1WPO
• 分子名称: PROTEASE, POTASSIUM ION (3 entities in total)
• 機能のキーワード: serine protease, antiviral drug design, capsid maturation, endopeptidase, assemblin, viral protein
• 由来する生物種: Human herpesvirus 8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50498.97

構造登録者

Reiling, K.K.,Pray, T.R.,Craik, C.S.,Stroud, R.M. (登録日: 2000-08-11, 公開日: 2000-11-22, 最終更新日: 2024-02-07)

主引用文献

Reiling, K.K.,Pray, T.R.,Craik, C.S.,Stroud, R.M.
Functional consequences of the Kaposi's sarcoma-associated herpesvirus protease structure: regulation of activity and dimerization by conserved structural elements.
Biochemistry, 39:12796-12803, 2000

PubMed Abstract: The structure of Kaposi's sarcoma-associated herpesvirus protease (KSHV Pr), at 2.2 A resolution, reveals the active-site geometry and defines multiple possible target sites for drug design against a human cancer-producing virus. The catalytic triad of KSHV Pr, (Ser114, His46, and His157) and transition-state stabilization site are arranged as in other structurally characterized herpesviral proteases. The distal histidine-histidine hydrogen bond is solvent accessible, unlike the situation in other classes of serine proteases. As in all herpesviral proteases, the enzyme is active only as a weakly associated dimer (K(d) approximately 2 microM), and inactive as a monomer. Therefore, both the active site and dimer interface are potential targets for antiviral drug design. The dimer interface in KSHV Pr is compared with the interface of other herpesviral proteases. Two conserved arginines (Arg209), one from each monomer, are buried within the same region of the dimer interface. We propose that this conserved arginine may provide a destabilizing element contributing to the tuned micromolar dissociation of herpesviral protease dimers.

PubMed: 11041844
DOI: 10.1021/bi001019h

実験手法

X-RAY DIFFRACTION (2.2 Å)