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Structural Studies of Herpesvirus Proteases

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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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Keywords: HERPESVIRUS PROTEASES; HHV7; HSV-2; Herpes simplex virus type 1 (HSV-1); Peptidomimetic inhibitors; Serine proteases; gamma herpesviruses; human cytomegalovirus (HCMV); human herpes virus 6 (HHV6); varicellar-zoster virus (VZV)

Document Type: Review Article

Affiliations: Department of Biological Sciences, Columbia University, New York, NY 10027, USA

Publication date: 2001-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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