1AVP

STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR

1AVP の概要

• エントリーDOI: 10.2210/pdb1avp/pdb
• 分子名称: ADENOVIRAL PROTEINASE (3 entities in total)
• 機能のキーワード: thiol hydrolase, viral proteinase, peptide cofactor, hydrolase
• 由来する生物種: Human adenovirus 2; 詳細
• 細胞内の位置: Virion : P03252; Pre-protein VI: Host nucleus . Endosome lysis protein: Virion : P03274
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24467.99

構造登録者

Ding, J.,Mcgrath, W.J.,Sweet, R.M.,Mangel, W.F. (登録日: 1996-04-04, 公開日: 1997-11-19, 最終更新日: 2024-11-20)

主引用文献

Ding, J.,McGrath, W.J.,Sweet, R.M.,Mangel, W.F.
Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor.
EMBO J., 15:1778-1783, 1996

PubMed Abstract: The three-dimensional structure of the human adenovirus-2 proteinase complexed with its 11 amino acid cofactor, pVIc, was determined at 2.6 A resolution by X-ray crystallographic analysis. The fold of this protein has not been seen before. However, it represents an example of either subtly divergent or powerfully convergent evolution, because the active site contains a Cys-His-Glu triplet and oxyanion hole in an arrangement similar to that in papain. Thus, the adenovirus proteinase represents a new, fifth group of enzymes that contain catalytic triads. pVIc, which extends a beta-sheet in the main chain, is distant from the active site, yet its binding increases the catalytic rate constant 300-fold for substrate hydrolysis. The structure reveals several potential targets for antiviral therapy.

PubMed: 8617222

実験手法

X-RAY DIFFRACTION (2.6 Å)