TY - JOUR
T1 - Inhibition of peptidyltransferase and possible mode of action of a dipeptidyl chloramphenicol analog
AU - McFarlan, Sara C.
AU - Vince, Robert
PY - 1984/7/31
Y1 - 1984/7/31
N2 - A dipeptidyl chloramphenicol analog, D-threo-2-(L-phenylalanylglycyl)amino-3-p-nitrophenyl-1,3-propanediol, has been prepared and examined as an inhibitor of ribosomal peptidyltransferase. The analog is a more effective inhibitor of poly (U,C) directed protein biosynthesis in an Escherichia coli cell-free system than chloramphenicol and shows inhibitory activity equal to the parent antibiotic in the transpeptidation reaction. These results and the common structural features of puromycin and this compound suggest a model for the binding modes of chloramphenicol and chloramphenicol analogs. This proposal invokes four major binding pockets at the A-site of the peptidyltransferase center.
AB - A dipeptidyl chloramphenicol analog, D-threo-2-(L-phenylalanylglycyl)amino-3-p-nitrophenyl-1,3-propanediol, has been prepared and examined as an inhibitor of ribosomal peptidyltransferase. The analog is a more effective inhibitor of poly (U,C) directed protein biosynthesis in an Escherichia coli cell-free system than chloramphenicol and shows inhibitory activity equal to the parent antibiotic in the transpeptidation reaction. These results and the common structural features of puromycin and this compound suggest a model for the binding modes of chloramphenicol and chloramphenicol analogs. This proposal invokes four major binding pockets at the A-site of the peptidyltransferase center.
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U2 - 10.1016/S0006-291X(84)80097-2
DO - 10.1016/S0006-291X(84)80097-2
M3 - Article
C2 - 6380501
AN - SCOPUS:0021201124
VL - 122
SP - 748
EP - 754
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -