Viral Proteases: Evolution of Diverse Structural Motifs to Optimize Function

• Published in: Cell Vol. 91; no. 4; pp. 427 - 430
• Main Authors: Babé, Lilia M, Craik, Charles S
• Format: Book Review Journal Article
• Language: English
• Published: United States Elsevier Inc 14.11.1997
• Subjects: Endopeptidases - chemistry; Evolution, Molecular; Models, Molecular; Viral Proteins - chemistry; Viruses - enzymology
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/S0092-8674(00)80426-2

There is more than one way to cleave a peptide bond, and viral proteases are revealing many new strategies for accomplishing the feat. As information on the three-dimensional structures and biological functions of viral proteases is obtained, unexpected protein folds and unique control mechanisms for proteolysis are being realized. These enzymes are teaching us a great deal about the various posttranslational modifications that occur during viral replication, and also about dramatic variations on the theme of proteolysis. Several viral proteases will be described here that exemplify the diversity of structures and biological functions displayed by these enzymes (Table 1). Viral and host proteases will be compared and contrasted to highlight the recent discovery of new protein folds, novel constellations of active-site residues, and unique allosteric mechanisms. Though not comprehensive, the following are some of the more striking examples of how viral proteases achieve and regulate their function during the multistep process of viral replication and maturation.