1887

Abstract

Computer-assisted comparison of the herpes simplex virus type 2 (HSV-2) ribonucleotide reductase large subunit (RR1) sequence with the known primary structures of other RR1 proteins revealed a motif consisting of five leucines occurring at every seventh residue between positions 409 to 437. This motif is specific to HSV RR1 proteins. A synthetic oligopeptide (LA-4) corresponding to 15 residues in the internal portion of the motif inhibited HSV-2 RR activity. In immunoprecipitation experiments, LA-4 disrupted a complex consisting of RR1, the small RR subunit and a previously uncharacterized 180K protein, apparently of cellular origin. We deduce that the LA-4 sequence represents a critical RR1 site involved in RR complex formation and enzymic activity.

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/content/journal/jgv/10.1099/0022-1317-72-5-1139
1991-05-01
2019-10-14
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-72-5-1139
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