1. Structure–activity relationships of ketolides vs. macrolides
S. Douthwaite 
Clinical Microbiology and Infection 
Volume 7, Pages (January 2001)
DOI: /j s3011.x
Copyright © 2001 European Society of Clinical Infectious Diseases Terms and Conditions

2. Fig 1 Ketolide and macrolide relationship.
Clinical Microbiology and Infection 2001 7, 11-17DOI: ( /j s3011.x)
Copyright © 2001 European Society of Clinical Infectious Diseases Terms and Conditions

3. Fig 2 Structure of the ketolide telithromycin.
Clinical Microbiology and Infection 2001 7, 11-17DOI: ( /j s3011.x)
Copyright © 2001 European Society of Clinical Infectious Diseases Terms and Conditions

4. Fig 3
(a) The drug binding site depicted on a portion of the 23S rRNA secondary structure model (Escherichia coli sequence). Nucleotides with which macrolide and ketolide drugs interact in domain II (upper) and domain V (lower) of the rRNA are circled. (b) The three-dimensional configuration of the drug binding site projected from the crystallographic coordinates of the 50S subunit (12). The encircled nucleotides in (a) are high-lighted in the portions of domain II (upper) and domain V (lower) shown here. The relative sizes of erythromycin (ery) and telithromycin (tel) illustrate how telithromycin can simultaneously interact with A752 in domain II and A2058 in domain V.
Clinical Microbiology and Infection 2001 7, 11-17DOI: ( /j s3011.x)
Copyright © 2001 European Society of Clinical Infectious Diseases Terms and Conditions

5. Fig 4
Binding curves for ketolides and macrolides to wild-type and A2058G mutant (MLSB-resistant) ribosomes. Mean (± SD)% base protection measured at A2058 and A2059 for wild-type ribosomes and at A2059 for A2058G mutant ribosomes. The degree of protection is taken to correspond to the proportion of ribosomes binding the drug, i.e. 0% = no binding; 100% = complete binding.
Clinical Microbiology and Infection 2001 7, 11-17DOI: ( /j s3011.x)
Copyright © 2001 European Society of Clinical Infectious Diseases Terms and Conditions