Abstract
Publisher Summary This chapter discusses structural features of protein prenylation and how these relate to the mechanisms of inhibition by small molecules. It also reviews recent structural studies of human pathogen protein prenyltransferases and how this information can be used for developing species-specific prenyltransferase inhibitors to treat infectious diseases. A family of structurally related protein prenyltransferase enzymes carries out protein prenylation: protein farnesyltransferase (FTase), protein geranylgeranyltransferase-I (GGTase-I), and Rab geranylgeranyltransferase (GGTase-II or Rab GGTase). This chapter describes the structural biology of Ca1a2X protein prenyltransferases (FTase and GGTase-I). These enzymes recognize a well-defined C-terminal motif on substrate proteins: cysteine (C), followed by two generally aliphatic amino acids (aa) and a variable (X) residue. Prenylated proteins play important signal transduction roles in all eukaryotes. Protein prenylation is critical for the growth and proliferation of pathogenic eukaryotic microorganisms, including the malaria protozoan Plasmodium falciparum. Protein prenyltransferases are attractive targets for the development of a number of therapeutics including cancer and infectious diseases caused by fungal and trypanosomatid pathogens.
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