Abstract
Structural studies of herpesvirus proteases establish that they belong to a new class of serine proteases and contain a novel Ser-His-His catalytic triad. Peptidomimetic inhibitors bind to the protease by forming an anti-parallel beeta-sheet with the enzyme. There are large conformational changes in the protease upon inhibitor binding, indicating that the protease is an induced-fit enzyme. Further studies are needed to understand the molecular basis for the dimerization requirement of the protease.
Keywords: HERPESVIRUS PROTEASES, Serine proteases, Peptidomimetic inhibitors, Herpes simplex virus type 1 (HSV-1), HSV-2, varicellar-zoster virus (VZV), human cytomegalovirus (HCMV), human herpes virus 6 (HHV6), HHV7, gamma herpesviruses
Protein & Peptide Letters
Title: Structural Studies of Herpesvirus Proteases
Volume: 8 Issue: 5
Author(s): Renu Batra, Reza Khayat and Liang Tong
Affiliation:
Keywords: HERPESVIRUS PROTEASES, Serine proteases, Peptidomimetic inhibitors, Herpes simplex virus type 1 (HSV-1), HSV-2, varicellar-zoster virus (VZV), human cytomegalovirus (HCMV), human herpes virus 6 (HHV6), HHV7, gamma herpesviruses
Abstract: Structural studies of herpesvirus proteases establish that they belong to a new class of serine proteases and contain a novel Ser-His-His catalytic triad. Peptidomimetic inhibitors bind to the protease by forming an anti-parallel beeta-sheet with the enzyme. There are large conformational changes in the protease upon inhibitor binding, indicating that the protease is an induced-fit enzyme. Further studies are needed to understand the molecular basis for the dimerization requirement of the protease.
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Cite this article as:
Batra Renu, Khayat Reza and Tong Liang, Structural Studies of Herpesvirus Proteases, Protein & Peptide Letters 2001; 8 (5) . https://dx.doi.org/10.2174/0929866013409229
DOI https://dx.doi.org/10.2174/0929866013409229 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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