1CMV

HUMAN CYTOMEGALOVIRUS PROTEASE

1CMV の概要

• エントリーDOI: 10.2210/pdb1cmv/pdb
• 分子名称: HUMAN CYTOMEGALOVIRUS PROTEASE (2 entities in total)
• 機能のキーワード: coat protein, hydrolase, serine protease, phosphorylation
• 由来する生物種: Human herpesvirus 5 (Human 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: 2
• 化学式量合計: 56142.96

構造登録者

Shieh, H.-S.,Kurumbail, R.G.,Stevens, A.M.,Stegeman, R.A.,Sturman, E.J.,Pak, J.Y.,Wittwer, A.J.,Palmier, M.O.,Wiegand, R.C.,Holwerda, B.C.,Stallings, W.C. (登録日: 1996-08-26, 公開日: 1997-09-04, 最終更新日: 2024-02-07)

主引用文献

Shieh, H.S.,Kurumbail, R.G.,Stevens, A.M.,Stegeman, R.A.,Sturman, E.J.,Pak, J.Y.,Wittwer, A.J.,Palmier, M.O.,Wiegand, R.C.,Holwerda, B.C.,Stallings, W.C.
Three-dimensional structure of human cytomegalovirus protease.
Nature, 383:279-282, 1996

PubMed Abstract: Herpesviruses encode a serine protease that specifically cleaves assembly protein. This protease is critical for replication, and represents a new target for antiviral drug design. Here we report the three-dimensional structure of the protease from human cytomegalovirus (hCMV) at 2.27 angstroms resolution. The structure reveals a unique fold and new catalytic strategy for cleavage. The monomer fold of the enzyme, a seven-stranded beta-barrel encircled by a chain of helices that form the carboxy terminus of the molecule, is unrelated to those observed in classic serine proteases such as chymotrypsin and subtilisin. The serine nucleophile at position 132 is activated by two juxtaposed histidine residues at positions 63 and 157. Dimerization, which seems to be necessary for activity, is observed in the crystals. Correlations of the structure with the sequences of herpesvirus proteases suggest that dimerization may confer specificity and recognition in substrate binding.

PubMed: 8805708
DOI: 10.1038/383279a0

実験手法

X-RAY DIFFRACTION (2.27 Å)