Abstract
The diversity of higher-order structure in ribonucleoprotein (RNP) complexes makes them amenable to small-molecule modulation of their biological function. This review will discuss why bacterial RNase P, a simple yet essential ubiquitous and highly conserved RNP enzyme, represents an excellent target for the discovery and development of novel antimicrobials.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
-
Review
MeSH terms
-
Animals
-
Anti-Infective Agents / pharmacology*
-
Enzyme Inhibitors / pharmacology*
-
Humans
-
Models, Molecular
-
Protein Subunits / metabolism
-
RNA, Bacterial / metabolism*
-
Ribonuclease P / antagonists & inhibitors*
-
Substrate Specificity
Substances
-
Anti-Infective Agents
-
Enzyme Inhibitors
-
Protein Subunits
-
RNA, Bacterial
-
Ribonuclease P