CONFORMATION OF 3'-NITRO-2',3'-DIDEOXYTHYMIDINE IN CRYSTAL AND SUBSTRATE PROPERTIES OF ITS 5'-TRIPHOSPHATE TOWARD REVERSE TRANSCRIPTASES

It was shown that the conformation of 3'-nitro-2',3'-dideoxythymidine in crystal is close to that of one of the 3'-azido-2',3'-dideoxythymid ine forms, This compound terminated DNA synthesis catalyzed by HN reve rse transcriptase, and the kinetic parameters of its incorporation int o the DNA chain were close to those for 3'-azido-2',3'-dideoxythymidin e 5'-triphosphate, 3'-Nitro-2',3'-dideoxythymidine 5'-triphosphate was less active toward avian myeloblastosis virus reverse transcriptase, and did not terminate DNA synthesis catalyzed by DNA polymerases or fr om human placenta and beta from rat liver, as well as herpes simplex v irus type 1 and human cytomegalovirus DNA polymerases and calf thymus terminal deoxynucleotidyl transferase.